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Conserved domains on  [gi|928147207|ref|XP_013972788|]
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neuronal-specific septin-3 isoform X2 [Canis lupus familiaris]

Protein Classification

septin family protein( domain architecture ID 10110922)

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

CATH:  3.40.50.300
Gene Ontology:  GO:0005525|GO:0003924|GO:0061640|GO:0060090
PubMed:  14611653|12445407|12111093|18478031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 496-769 2.13e-173

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: 499.38  E-value: 2.13e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 496 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 575
Cdd:cd01850    2 GFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 576 WEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 655
Cdd:cd01850   82 WKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 656 EFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFAL 735
Cdd:cd01850  162 EFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFVK 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 928147207 736 LRDFVIRTHLQDLKEVTHNIHYETYRAKRLNDNG 769
Cdd:cd01850  242 LRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 35-468 2.53e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207   35 SGGMSPLIPVLRKTISLDTFTQShiPQASSRP---GLGARAR--SVPPQETVPRKLSSISLTLRQNSQAWPLGPLPSHWE 109
Cdd:PHA03247 2548 AGDPPPPLPPAAPPAAPDRSVPP--PRPAPRPsepAVTSRARrpDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPD 2625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  110 EPPTVGREAATHGGGRLPTPGsrlgsttlvsggrvysegpgnPGLAKPSRMPIVekPLVSSYLSLPFQSRLAQKSPGPAG 189
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTV---------------------PPPERPRDDPAP--GRVSRPRRARRLGRAAQASSPPQR 2682

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  190 PGSVGQKHPVpvtAHVTTRASPGRGKPRARgiPRPRLHLQRGTSTMGPAMAmdlatldttrlGTARRLTTVVTNRPDLTI 269
Cdd:PHA03247 2683 PRRRAARPTV---GSLTSLADPPPPPPTPE--PAPHALVSATPLPPGPAAA-----------RQASPALPAAPAPPAVPA 2746

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  270 NPATPSTSRLDTSTEFPALDPKPGMAVDLAAAGPAKLgmvmdlvdpdkLVKVIATAGAAKSDTTTGGMAMDLVVPAPAKL 349
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL-----------TRPAVASLSESRESLPSPWDPADPPAAVLAPA 2815

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  350 DTARTDTAMALARANTARLDITADSFASDTSKLGTVMGetmldrvinltvSATYPLMPSRSTNPALDHATADAATDRsik 429
Cdd:PHA03247 2816 AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG------------GSVAPGGDVRRRPPSRSPAAKPAAPAR--- 2880

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 928147207  430 PVMLNLARESkgLPEARTDAAMSELVPEPRPKPAVPMKP 468
Cdd:PHA03247 2881 PPVRRLARPA--VSRSTESFALPPDQPERPPQPQAPPPP 2917
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 496-769 2.13e-173

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: 499.38  E-value: 2.13e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 496 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 575
Cdd:cd01850    2 GFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 576 WEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 655
Cdd:cd01850   82 WKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 656 EFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFAL 735
Cdd:cd01850  162 EFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFVK 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 928147207 736 LRDFVIRTHLQDLKEVTHNIHYETYRAKRLNDNG 769
Cdd:cd01850  242 LRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 496-765 3.22e-145

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: 427.10  E-value: 3.22e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  496 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 575
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  576 WEPIEKYINEQYEKFLKEEVNIARKKRIpDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 655
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  656 EFKQRVRKELEVNGIEFY--PQKEFDEDlEDKTENDKIRESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEF 733
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYhfPDEESDED-EEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 928147207  734 ALLRDFVIRTHLQDLKEVTHNIHYETYRAKRL 765
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 476-765 9.42e-136

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 407.09  E-value: 9.42e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 476 LGYIGIDTIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLF-KSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGV 554
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFgTSLVDETEIDDIRAEGTSPTLEIKITKAELEEDGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 555 KMKLTVIDTPGFGDQINNENCWEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLS 634
Cdd:COG5019   81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 635 KVVNIIPVIAKADTMTLEEKSEFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDK-IRESMPFAVVGSDKEYQVNGKRV 713
Cdd:COG5019  161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLEENQdLRSLIPFAIIGSNTEIENGGEQV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 928147207 714 LGRKTPWGIIEVENLNHCEFALLRDFVIRTHLQDLKEVTHNIHYETYRAKRL 765
Cdd:COG5019  241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL 292
PHA03247 PHA03247
large tegument protein UL36; Provisional
 35-468 2.53e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207   35 SGGMSPLIPVLRKTISLDTFTQShiPQASSRP---GLGARAR--SVPPQETVPRKLSSISLTLRQNSQAWPLGPLPSHWE 109
Cdd:PHA03247 2548 AGDPPPPLPPAAPPAAPDRSVPP--PRPAPRPsepAVTSRARrpDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPD 2625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  110 EPPTVGREAATHGGGRLPTPGsrlgsttlvsggrvysegpgnPGLAKPSRMPIVekPLVSSYLSLPFQSRLAQKSPGPAG 189
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTV---------------------PPPERPRDDPAP--GRVSRPRRARRLGRAAQASSPPQR 2682

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  190 PGSVGQKHPVpvtAHVTTRASPGRGKPRARgiPRPRLHLQRGTSTMGPAMAmdlatldttrlGTARRLTTVVTNRPDLTI 269
Cdd:PHA03247 2683 PRRRAARPTV---GSLTSLADPPPPPPTPE--PAPHALVSATPLPPGPAAA-----------RQASPALPAAPAPPAVPA 2746

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  270 NPATPSTSRLDTSTEFPALDPKPGMAVDLAAAGPAKLgmvmdlvdpdkLVKVIATAGAAKSDTTTGGMAMDLVVPAPAKL 349
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL-----------TRPAVASLSESRESLPSPWDPADPPAAVLAPA 2815

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  350 DTARTDTAMALARANTARLDITADSFASDTSKLGTVMGetmldrvinltvSATYPLMPSRSTNPALDHATADAATDRsik 429
Cdd:PHA03247 2816 AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG------------GSVAPGGDVRRRPPSRSPAAKPAAPAR--- 2880

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 928147207  430 PVMLNLARESkgLPEARTDAAMSELVPEPRPKPAVPMKP 468
Cdd:PHA03247 2881 PPVRRLARPA--VSRSTESFALPPDQPERPPQPQAPPPP 2917
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 498-565 3.47e-05

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 44.67  E-value: 3.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928147207  498 DFNIMVVGQSGLGKSTLVNTLFKSQVSrkasswnrEEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPG 565
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGS--------ITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAG 60
TIN2_TBM cd11741
TRF-binding motif region of TRF-Interacting Nuclear factor 2; The C-terminal region of TIN2 ...
 197-255 7.95e-03

TRF-binding motif region of TRF-Interacting Nuclear factor 2; The C-terminal region of TIN2 contains the TRF-binding motif (TBM), while the TIN2 N-terminal region acts in the modulation of TRF1 activity via the inhibition of tankyrase 1. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) and the N-terminus, while the far C-terminal region interacts with lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a a negative regulatory function of this region. TIN2 is a shelterin complex protein identified in mammals, one of 6 factors that act to protect telomeres from DNA damage repair machinery. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of SCF complexes (SCF: Skp1-Cul1-Rbx1-F- box protein). Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds TPP1, which recruits POT1 to telomeres.


Pssm-ID: 240666 [Multi-domain]  Cd Length: 108  Bit Score: 36.72  E-value: 7.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 928147207 197 HPVPVTAHVTTRASPGRGKPRARGIPRPRLHLQRGTSTMGPAMAMDLATLDTTRLGTAR 255
Cdd:cd11741    1 PPSSLTGRGFGLAPLSKRKSQSRWPSAPRSHKERPTTMLPPRRSTKLPTQKPSRSPASR 59
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
 496-769 2.13e-173

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: 499.38  E-value: 2.13e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 496 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 575
Cdd:cd01850    2 GFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSDC 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 576 WEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 655
Cdd:cd01850   82 WKPIVDYIDDQFESYLREESRINRNRRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEELT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 656 EFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDKIRESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEFAL 735
Cdd:cd01850  162 EFKKRIMEDIEENNIKIYKFPEDEEDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDFVK 241

                        250       260       270
                 ....*....|....*....|....*....|....
gi 928147207 736 LRDFVIRTHLQDLKEVTHNIHYETYRAKRLNDNG 769
Cdd:cd01850  242 LRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
 496-765 3.22e-145

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: 427.10  E-value: 3.22e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  496 GFDFNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGFGDQINNENC 575
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARGIPGPSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  576 WEPIEKYINEQYEKFLKEEVNIARKKRIpDTRVHCCLYFISPTGHSLRPLDLEFMKHLSKVVNIIPVIAKADTMTLEEKS 655
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNRKSIK-DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDELQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  656 EFKQRVRKELEVNGIEFY--PQKEFDEDlEDKTENDKIRESMPFAVVGSDKEYQVNGKRVLGRKTPWGIIEVENLNHCEF 733
Cdd:pfam00735 160 RFKKRIREEIERQNIPIYhfPDEESDED-EEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 928147207  734 ALLRDFVIRTHLQDLKEVTHNIHYETYRAKRL 765
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKL 270
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
 476-765 9.42e-136

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 407.09  E-value: 9.42e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 476 LGYIGIDTIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLF-KSQVSRKASSWNREEKIPKTVEIKAIGHVIEEGGV 554
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFgTSLVDETEIDDIRAEGTSPTLEIKITKAELEEDGF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 555 KMKLTVIDTPGFGDQINNENCWEPIEKYINEQYEKFLKEEVNIARKKRIPDTRVHCCLYFISPTGHSLRPLDLEFMKHLS 634
Cdd:COG5019   81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRLS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 635 KVVNIIPVIAKADTMTLEEKSEFKQRVRKELEVNGIEFYPQKEFDEDLEDKTENDK-IRESMPFAVVGSDKEYQVNGKRV 713
Cdd:COG5019  161 KRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDPYDPEDDEDESLEENQdLRSLIPFAIIGSNTEIENGGEQV 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 928147207 714 LGRKTPWGIIEVENLNHCEFALLRDFVIRTHLQDLKEVTHNIHYETYRAKRL 765
Cdd:COG5019  241 RGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL 292
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 503-674 2.27e-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: 54.00  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 503 VVGQSGLGKSTLVNTLFKSQVSRKasswnrEEKIPKTVEIKAIGHVIEEGGVkmKLTVIDTPGFGDqINNENCWEPIEKY 582
Cdd:cd00882    2 VVGRGGVGKSSLLNALLGGEVGEV------SDVPGTTRDPDVYVKELDKGKV--KLVLVDTPGLDE-FGGLGREELARLL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 583 INeqyekflkeevniarkkripdtRVHCCLYFISPTGH-SLRPLDLEFMKHLSKV-VNIIPVIAKADTMTLEEKSEFKQR 660
Cdd:cd00882   73 LR----------------------GADLILLVVDSTDReSEEDAKLLILRRLRKEgIPIILVGNKIDLLEEREVEELLRL 130

                        170
                 ....*....|....
gi 928147207 661 VRKELEvNGIEFYP 674
Cdd:cd00882  131 EELAKI-LGVPVFE 143
Toc34_like cd01853
Translocon at the Outer-envelope membrane of Chloroplasts 34-like (Toc34-like); The Toc34-like ...
 485-614 5.04e-08

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: 54.63  E-value: 5.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 485 IEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLF---KSQVSRKASSWNREEKIPKTVeikaighvieeGGVkmKLTVI 561
Cdd:cd01853   18 HELEAKLKKELDFSLTILVLGKTGVGKSSTINSIFgerKVSVSAFQSETLRPREVSRTV-----------DGF--KLNII 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 928147207 562 DTPGF---GDQINNENCWEPIEKYIneqyekflkeevniarKKRIPDtrvhCCLYF 614
Cdd:cd01853   85 DTPGLlesQDQRVNRKILSIIKRFL----------------KKKTID----VVLYV 120
YeeP COG3596
Predicted GTPase [General function prediction only];
483-644 2.35e-07

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 53.23  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 483 TIIEQMRKKTMKTGFDFNIMVVGQSGLGKSTLVNTLFKSQVSRkasswnREEKIPKTVEIKAigHVIEEGGVKMkLTVID 562
Cdd:COG3596   24 ELLAEALERLLVELPPPVIALVGKTGAGKSSLINALFGAEVAE------VGVGRPCTREIQR--YRLESDGLPG-LVLLD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 563 TPGFGDQINNEncwepiEKYIneQYEKFLKEevniarkkripdtrVHCCLYFISPTGHSLRpLDLEFMKHLSKVVNIIPV 642
Cdd:COG3596   95 TPGLGEVNERD------REYR--ELRELLPE--------------ADLILWVVKADDRALA-TDEEFLQALRAQYPDPPV 151


                 ..
gi 928147207 643 IA 644
Cdd:COG3596  152 LV 153
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
 479-566 3.25e-07

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ 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. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 51.63  E-value: 3.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 479 IGIDTIIEQMRKKTmktgfdfnIMVVGQSGLGKSTLVNTLFKsqvsrkasswnrEEKIpKTVEI-KAIG----------- 546
Cdd:cd01854   74 EGLDELRELLKGKT--------SVLVGQSGVGKSTLLNALLP------------ELVL-ATGEIsEKLGrgrhttthrel 132

                         90       100
                 ....*....|....*....|
gi 928147207 547 HVIEEGGVkmkltVIDTPGF 566
Cdd:cd01854  133 FPLPGGGL-----IIDTPGF 147
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 500-643 5.36e-06

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: 46.07  E-value: 5.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  500 NIMVVGQSGLGKSTLVNTLF--KSQVSRKAsswnreekiPKTVEIkaIGHVIEEGGVKMKLtvIDTPGFgdqinnencwe 577
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTgaKAIVSDYP---------GTTRDP--NEGRLELKGKQIIL--VDTPGL----------- 56

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928147207  578 piekyineqYEKFLKEEVNIARKKRIPDTRVhccLYFISPTGHSLRPLDLEFMKHLSKvvNIIPVI 643
Cdd:pfam01926  57 ---------IEGASEGEGLGRAFLAIIEADL---ILFVVDSEEGITPLDEELLELLRE--NKKPII 108
RsgA COG1162
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
479-566 6.60e-06

Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440776 [Multi-domain]  Cd Length: 300  Bit Score: 48.57  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 479 IGIDTIIEQMRKKTmktgfdfnIMVVGQSGLGKSTLVNTLFKsqvsrkasswnrEEKIpKTVEI-KAIG----------- 546
Cdd:COG1162  155 EGLDELRELLKGKT--------SVLVGQSGVGKSTLINALLP------------DADL-ATGEIsEKLGrgrhttthael 213

                         90       100
                 ....*....|....*....|
gi 928147207 547 HVIEEGGVkmkltVIDTPGF 566
Cdd:COG1162  214 YPLPGGGW-----LIDTPGF 228
PHA03247 PHA03247
large tegument protein UL36; Provisional
 35-468 2.53e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207   35 SGGMSPLIPVLRKTISLDTFTQShiPQASSRP---GLGARAR--SVPPQETVPRKLSSISLTLRQNSQAWPLGPLPSHWE 109
Cdd:PHA03247 2548 AGDPPPPLPPAAPPAAPDRSVPP--PRPAPRPsepAVTSRARrpDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPD 2625

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  110 EPPTVGREAATHGGGRLPTPGsrlgsttlvsggrvysegpgnPGLAKPSRMPIVekPLVSSYLSLPFQSRLAQKSPGPAG 189
Cdd:PHA03247 2626 PPPPSPSPAANEPDPHPPPTV---------------------PPPERPRDDPAP--GRVSRPRRARRLGRAAQASSPPQR 2682

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  190 PGSVGQKHPVpvtAHVTTRASPGRGKPRARgiPRPRLHLQRGTSTMGPAMAmdlatldttrlGTARRLTTVVTNRPDLTI 269
Cdd:PHA03247 2683 PRRRAARPTV---GSLTSLADPPPPPPTPE--PAPHALVSATPLPPGPAAA-----------RQASPALPAAPAPPAVPA 2746

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  270 NPATPSTSRLDTSTEFPALDPKPGMAVDLAAAGPAKLgmvmdlvdpdkLVKVIATAGAAKSDTTTGGMAMDLVVPAPAKL 349
Cdd:PHA03247 2747 GPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRRL-----------TRPAVASLSESRESLPSPWDPADPPAAVLAPA 2815

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  350 DTARTDTAMALARANTARLDITADSFASDTSKLGTVMGetmldrvinltvSATYPLMPSRSTNPALDHATADAATDRsik 429
Cdd:PHA03247 2816 AALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLG------------GSVAPGGDVRRRPPSRSPAAKPAAPAR--- 2880

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 928147207  430 PVMLNLARESkgLPEARTDAAMSELVPEPRPKPAVPMKP 468
Cdd:PHA03247 2881 PPVRRLARPA--VSRSTESFALPPDQPERPPQPQAPPPP 2917
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 498-565 3.47e-05

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 44.67  E-value: 3.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928147207  498 DFNIMVVGQSGLGKSTLVNTLFKSQVSrkasswnrEEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPG 565
Cdd:TIGR00231   1 DIKIVIVGHPNVGKSTLLNSLLGNKGS--------ITEYYPGTTRNYVTTVIEEDGKTYKFNLLDTAG 60
YqeH cd01855
Circularly permuted YqeH GTPase; YqeH is an essential GTP-binding protein. Depletion of YqeH ...
 469-566 5.29e-05

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: 44.95  E-value: 5.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 469 VSINSNLLGYiGIDTIIEQMRKKTMKTGfdfNIMVVGQSGLGKSTLVNTLFKSQVSRKASSWNREE----KIP-KTVEIK 543
Cdd:cd01855  100 VILVSAKKGW-GVEELIEEIKKLAKYRG---DVYVVGATNVGKSTLINALLKSNGGKVQAQALVQRltvsPIPgTTLGLI 175

                         90       100
                 ....*....|....*....|...
gi 928147207 544 AIghvieegGVKMKLTVIDTPGF 566
Cdd:cd01855  176 KI-------PLGEGKKLYDTPGI 191
3a0901s04IAP86 TIGR00993
chloroplast protein import component Toc86/159, G and M domains; The long precursor of the 86K ...
 497-583 3.38e-04

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: 44.17  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  497 FDFNIMVVGQSGLGKSTLVNTLFKSQvsrKASSwnrEEKIPKTVEIKAIghvieEGGVK-MKLTVIDTPGF----GDQIN 571
Cdd:TIGR00993 117 FSLNILVLGKSGVGKSATINSIFGEV---KFST---DAFGMGTTSVQEI-----EGLVQgVKIRVIDTPGLkssaSDQSK 185

                          90
                  ....*....|..
gi 928147207  572 NENCWEPIEKYI 583
Cdd:TIGR00993 186 NEKILSSVKKFI 197
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 503-568 4.02e-04

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that 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. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 41.85  E-value: 4.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928147207 503 VVGQSGLGKSTLVNTLFKSQVSrKASSWNREEKIPKTVEIKaighVIEEGGVkmklTVIDTPGFGD 568
Cdd:cd00880    2 IFGRPNVGKSSLLNALLGQNVG-IVSPIPGTTRDPVRKEWE----LLPLGPV----VLIDTPGLDE 58
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
501-673 4.38e-04

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 41.89  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 501 IMVVGQSGLGKSTLVNTLFKSQVSrkasswnrEEKIPKTVEIKAIGHVIEEGGVKMKLTVIDTPGfgdqinnencwepIE 580
Cdd:COG1100    6 IVVVGTGGVGKTSLVNRLVGDIFS--------LEKYLSTNGVTIDKKELKLDGLDVDLVIWDTPG-------------QD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207 581 KY--INEQYEKFLKEevniarkkripdtrVHCCLYFISPT-GHSLRPLD--LEFMKHLSKVVNIIPVIAKADTMTLEEKS 655
Cdd:COG1100   65 EFreTRQFYARQLTG--------------ASLYLFVVDGTrEETLQSLYelLESLRRLGKKSPIILVLNKIDLYDEEEIE 130

                        170
                 ....*....|....*...
gi 928147207 656 EfKQRVRKELEVNGIEFY 673
Cdd:COG1100  131 D-EERLKEALSEDNIVEV 147
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
 479-566 2.33e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 39.83  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  479 IGIDTIIEQMRKKTmktgfdfnIMVVGQSGLGKSTLVNTLFKSQVSRKA---SSWNREEKIPKTVEIkaigHVIEEGGVk 555
Cdd:pfam03193  95 EGIEALKELLKGKT--------TVLAGQSGVGKSTLLNALLPELDLRTGeisEKLGRGRHTTTHVEL----FPLPGGGL- 161

                          90
                  ....*....|.
gi 928147207  556 mkltVIDTPGF 566
Cdd:pfam03193 162 ----LIDTPGF 168
PHA03247 PHA03247
large tegument protein UL36; Provisional
 28-292 7.02e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 40.31  E-value: 7.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207   28 PARPSKLSGGMSPLIPVLRKTISLDTFTQSHIPQASSRPGLGARARSVPPQETVPRKLSSISLTLRQNSQAWPLGPL--P 105
Cdd:PHA03247 2601 PVDDRGDPRGPAPPSPLPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASspP 2680

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  106 SHWEE---PPTVGREAAThggGRLPTPgsrlgsttlvsggrvysegPGNPGLAKPSRMPIVEKPLVSSYLSLPFQSRLAQ 182
Cdd:PHA03247 2681 QRPRRraaRPTVGSLTSL---ADPPPP-------------------PPTPEPAPHALVSATPLPPGPAAARQASPALPAA 2738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  183 KSPGPAGPGSVGQKHPVPVTAHVTTRASPGRGKPRARGIPRPRlhlqrgtSTMGPAMAMDLATLDTTRLGTARRLTTVVT 262
Cdd:PHA03247 2739 PAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPR-------RLTRPAVASLSESRESLPSPWDPADPPAAV 2811

                         250       260       270
                  ....*....|....*....|....*....|.
gi 928147207  263 NRPDLTINP-ATPSTSRLDTSTEFPALDPKP 292
Cdd:PHA03247 2812 LAPAAALPPaASPAGPLPPPTSAQPTAPPPP 2842
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 9-238 7.42e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 40.15  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207    9 QHGAPSPGTSLSHSHLLGRPARPSKLSGGMSPLIPVLRKTISLDtftqshipqaSSRPGLGARARSVPPQETVPRKLSSI 88
Cdd:PHA03307  203 SPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSG----------CGWGPENECPLPRPAPITLPTRIWEA 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207   89 SLTLRQNSQAwplGPLPSHWEEPPTVGREAATHGGGRLPTPGSRLGSttlvsggrvYSEGPGNPGLAKPSRMPIVEKPLV 168
Cdd:PHA03307  273 SGWNGPSSRP---GPASSSSSPRERSPSPSPSSPGSGPAPSSPRASS---------SSSSSRESSSSSTSSSSESSRGAA 340

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928147207  169 SSYLSLPFQSRLAQKSPGPAGPGSVGQKHPvPVTAHVTTRASPGRGKPRARGIPRPRLHLQRGTSTMGPA 238
Cdd:PHA03307  341 VSPGPSPSRSPSPSRPPPPADPSSPRKRPR-PSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFPA 409
TIN2_TBM cd11741
TRF-binding motif region of TRF-Interacting Nuclear factor 2; The C-terminal region of TIN2 ...
 197-255 7.95e-03

TRF-binding motif region of TRF-Interacting Nuclear factor 2; The C-terminal region of TIN2 contains the TRF-binding motif (TBM), while the TIN2 N-terminal region acts in the modulation of TRF1 activity via the inhibition of tankyrase 1. TIN2 binding to TRF2 is primarily via the TRF binding motif (TBM) and the N-terminus, while the far C-terminal region interacts with lower affinity. The TIN2 TBM, but not the N-terminal region, is involved in TIN2 binding to TRF1. Truncation of the TIN2 N-terminus in mouse results in telomere elongation, suggesting a a negative regulatory function of this region. TIN2 is a shelterin complex protein identified in mammals, one of 6 factors that act to protect telomeres from DNA damage repair machinery. Three shelterin components (TRF1, TRF2, POT1) bind DNA and 3 components (TIN2, RAP1, TPP1) are recruited by these DNA binding factors. TIN2 binds directly to TRF1 and TRF2 and stabilizes TRF2 complex-telomere binding by tethering it to the TRF1 complex. TRF1 activity at telomeres is regulated in part by selective ubiquitination and degradation. Ubiquitination of TRF1 is mediated by Fbx4, which binds TRF1 in the TRFH domain, via a small GTPase module. When bound to telomeres, TIN2 acts to protect TRF1 from SCF-Fbx4 mediated ubiquitination. F-box proteins act in substrate recognition as part of SCF complexes (SCF: Skp1-Cul1-Rbx1-F- box protein). Tankyrase-mediated ADP-ribosylation releases TRF1 from telomeres, rendering them susceptible to ubiquitination and degradation, promoting telomere elongation. TIN2 also binds TPP1, which recruits POT1 to telomeres.


Pssm-ID: 240666 [Multi-domain]  Cd Length: 108  Bit Score: 36.72  E-value: 7.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 928147207 197 HPVPVTAHVTTRASPGRGKPRARGIPRPRLHLQRGTSTMGPAMAMDLATLDTTRLGTAR 255
Cdd:cd11741    1 PPSSLTGRGFGLAPLSKRKSQSRWPSAPRSHKERPTTMLPPRRSTKLPTQKPSRSPASR 59
 
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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