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Conserved domains on  [gi|564397859|ref|XP_006256479|]
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septin-10 isoform X3 [Rattus norvegicus]

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

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 ...
36-304 3.88e-140

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: 402.31  E-value: 3.88e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  36 QGFCFNILCVGETGIGKSTLINTLFNTNF-----EELESSHFCPCVRLRAQTYELQESNVRLKLTIVNTVGFGDQINKEE 110
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLypskyPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 111 SYQPIVDYIDNQFEAYLQEELKIKRALfNYHDSRIHVCLYFIAPTGHSLRTLDLLTMKSLDNKVNIIPLIAKADTISKSE 190
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNR-RIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 191 LQKFKMKLMSELVINGVQIYQFPTD--DDTTAKINGAMNGHLPFAVVGSMDEIKVGNKMVKARQYPWGIVQVENENHCDF 268
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564397859 269 VKLREMLICTNMEDLREQTHMRHYELYRRCKLQEMG 304
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
DUF5401 super family cl38662
Family of unknown function (DUF5401); This is a family of unknown function found in ...
242-385 4.65e-04

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


The actual alignment was detected with superfamily member pfam17380:

Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  242 KVGNKMVKARQYPWGIVQVENENHCDFVKLREMLICTNMEDLREQTHMRhyelyRRCKL----QEMGFIDIGPENKPLSL 317
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLelekEKRDRKRAEEQRRKILE 498
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  318 QETYEAKRHEFCGERQRK--EEQMKQMFVQRVKEKEAILKEAERELQAKFEHLKRIHQEERMKLEEKRRM 385
Cdd:pfam17380 499 KELEERKQAMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL 568
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
36-304 3.88e-140

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: 402.31  E-value: 3.88e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  36 QGFCFNILCVGETGIGKSTLINTLFNTNF-----EELESSHFCPCVRLRAQTYELQESNVRLKLTIVNTVGFGDQINKEE 110
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLypskyPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 111 SYQPIVDYIDNQFEAYLQEELKIKRALfNYHDSRIHVCLYFIAPTGHSLRTLDLLTMKSLDNKVNIIPLIAKADTISKSE 190
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNR-RIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 191 LQKFKMKLMSELVINGVQIYQFPTD--DDTTAKINGAMNGHLPFAVVGSMDEIKVGNKMVKARQYPWGIVQVENENHCDF 268
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564397859 269 VKLREMLICTNMEDLREQTHMRHYELYRRCKLQEMG 304
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
37-302 4.34e-110

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: 325.79  E-value: 4.34e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859   37 GFCFNILCVGETGIGKSTLINTLFNTNFEElESSHFCPC------VRLRAQTYELQESNVRLKLTIVNTVGFGDQINKEE 110
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYR-ARGIPGPSekikktVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  111 SYQPIVDYIDNQFEAYLQEELKIKRALFNyhDSRIHVCLYFIAPTGHSLRTLDLLTMKSLDNKVNIIPLIAKADTISKSE 190
Cdd:pfam00735  80 CWRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  191 LQKFKMKLMSELVINGVQIYQFP---TDDDTTAKINGAMNGHLPFAVVGSMDEIKVGNKMVKARQYPWGIVQVENENHCD 267
Cdd:pfam00735 158 LQRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCD 237
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 564397859  268 FVKLREMLICTNMEDLREQTHMRHYELYRRCKLQE 302
Cdd:pfam00735 238 FLKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
17-389 1.29e-105

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 318.11  E-value: 1.29e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  17 CGHVGFESLPDQLVDRSIEQGFCFNILCVGETGIGKSTLINTLFNT------NFEELESSHFCPCVRLRAQTYELQESNV 90
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTslvdetEIDDIRAEGTSPTLEIKITKAELEEDGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  91 RLKLTIVNTVGFGDQINKEESYQPIVDYIDNQFEAYLQEELKIKRALFnYHDSRIHVCLYFIAPTGHSLRTLDLLTMKSL 170
Cdd:COG5019   81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 171 DNKVNIIPLIAKADTISKSELQKFKMKLMSELVINGVQIYQ-FPTDDDTTAKI--NGAMNGHLPFAVVGSMDEIKVGNKM 247
Cdd:COG5019  160 SKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLeeNQDLRSLIPFAIIGSNTEIENGGEQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 248 VKARQYPWGIVQVENENHCDFVKLREMLICTNMEDLREQTHMRHYELYRRCKLqemgfidigpenkpLSLQETYEAKRHE 327
Cdd:COG5019  240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL--------------SGLKNSGEPSLKE 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564397859 328 FCGERQRKEE-QMKQMFVQRVKEKEAILKEAERELQAKFEHLKRIHQEERMKLEEKRRMLEEE 389
Cdd:COG5019  306 IHEARLNEEErELKKKFTEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKL 368
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
242-385 4.65e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  242 KVGNKMVKARQYPWGIVQVENENHCDFVKLREMLICTNMEDLREQTHMRhyelyRRCKL----QEMGFIDIGPENKPLSL 317
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLelekEKRDRKRAEEQRRKILE 498
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  318 QETYEAKRHEFCGERQRK--EEQMKQMFVQRVKEKEAILKEAERELQAKFEHLKRIHQEERMKLEEKRRM 385
Cdd:pfam17380 499 KELEERKQAMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL 568
PTZ00121 PTZ00121
MAEBL; Provisional
331-422 2.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  331 ERQRKEEQMKQMFVQRVKEKEAiLKEAERELQAKFEHLKRIHQEERMKLEEKRRMlEEESVAFAKKKATCELFPHQSFLA 410
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEE-LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKE 1776
                          90
                  ....*....|..
gi 564397859  411 SGSSIRRDKDRK 422
Cdd:PTZ00121 1777 KEAVIEEELDEE 1788
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
333-389 3.70e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.10  E-value: 3.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564397859 333 QRKEEQMKQMFVQRVKEKEA-----ILKEAERELQAKFEHLKRIHQEE----RMKLEEKRRMLEEE 389
Cdd:cd16269  191 QALTEKEKEIEAERAKAEAAeqerkLLEEQQRELEQKLEDQERSYEEHlrqlKEKMEEERENLLKE 256
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
317-396 8.00e-03

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


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 36.69  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 317 LQETYEAKRHEFCGERQRKEEQMKQmfvQRVKEKEAILKEAERELQAKFEH-LKRIHQEERMKLEEKRRMLEEESVAFAK 395
Cdd:COG0711   53 ALAEYEEKLAEARAEAAEIIAEARK---EAEAIAEEAKAEAEAEAERIIAQaEAEIEQERAKALAELRAEVADLAVAIAE 129

                 .
gi 564397859 396 K 396
Cdd:COG0711  130 K 130
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
36-304 3.88e-140

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: 402.31  E-value: 3.88e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  36 QGFCFNILCVGETGIGKSTLINTLFNTNF-----EELESSHFCPCVRLRAQTYELQESNVRLKLTIVNTVGFGDQINKEE 110
Cdd:cd01850    1 RGFQFNIMVVGESGLGKSTFINTLFGTKLypskyPPAPGEHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 111 SYQPIVDYIDNQFEAYLQEELKIKRALfNYHDSRIHVCLYFIAPTGHSLRTLDLLTMKSLDNKVNIIPLIAKADTISKSE 190
Cdd:cd01850   81 CWKPIVDYIDDQFESYLREESRINRNR-RIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 191 LQKFKMKLMSELVINGVQIYQFPTD--DDTTAKINGAMNGHLPFAVVGSMDEIKVGNKMVKARQYPWGIVQVENENHCDF 268
Cdd:cd01850  160 LTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564397859 269 VKLREMLICTNMEDLREQTHMRHYELYRRCKLQEMG 304
Cdd:cd01850  240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
37-302 4.34e-110

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: 325.79  E-value: 4.34e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859   37 GFCFNILCVGETGIGKSTLINTLFNTNFEElESSHFCPC------VRLRAQTYELQESNVRLKLTIVNTVGFGDQINKEE 110
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYR-ARGIPGPSekikktVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  111 SYQPIVDYIDNQFEAYLQEELKIKRALFNyhDSRIHVCLYFIAPTGHSLRTLDLLTMKSLDNKVNIIPLIAKADTISKSE 190
Cdd:pfam00735  80 CWRPIVEYIDEQYEQYLRDESGLNRKSIK--DNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  191 LQKFKMKLMSELVINGVQIYQFP---TDDDTTAKINGAMNGHLPFAVVGSMDEIKVGNKMVKARQYPWGIVQVENENHCD 267
Cdd:pfam00735 158 LQRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCD 237
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 564397859  268 FVKLREMLICTNMEDLREQTHMRHYELYRRCKLQE 302
Cdd:pfam00735 238 FLKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
17-389 1.29e-105

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 318.11  E-value: 1.29e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  17 CGHVGFESLPDQLVDRSIEQGFCFNILCVGETGIGKSTLINTLFNT------NFEELESSHFCPCVRLRAQTYELQESNV 90
Cdd:COG5019    1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTslvdetEIDDIRAEGTSPTLEIKITKAELEEDGF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  91 RLKLTIVNTVGFGDQINKEESYQPIVDYIDNQFEAYLQEELKIKRALFnYHDSRIHVCLYFIAPTGHSLRTLDLLTMKSL 170
Cdd:COG5019   81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRNPK-FKDTRVHACLYFIRPTGHGLKPLDIEAMKRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 171 DNKVNIIPLIAKADTISKSELQKFKMKLMSELVINGVQIYQ-FPTDDDTTAKI--NGAMNGHLPFAVVGSMDEIKVGNKM 247
Cdd:COG5019  160 SKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLeeNQDLRSLIPFAIIGSNTEIENGGEQ 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 248 VKARQYPWGIVQVENENHCDFVKLREMLICTNMEDLREQTHMRHYELYRRCKLqemgfidigpenkpLSLQETYEAKRHE 327
Cdd:COG5019  240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKL--------------SGLKNSGEPSLKE 305
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564397859 328 FCGERQRKEE-QMKQMFVQRVKEKEAILKEAERELQAKFEHLKRIHQEERMKLEEKRRMLEEE 389
Cdd:COG5019  306 IHEARLNEEErELKKKFTEKIREKEKRLEELEQNLIEERKELNSKLEEIQKKLEDLEKRLEKL 368
YeeP COG3596
Predicted GTPase [General function prediction only];
40-121 2.66e-10

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 61.32  E-value: 2.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  40 FNILCVGETGIGKSTLINTLFNTNFEELesSHFCPCVRlRAQTYELQESNVRLkLTIVNTVGFGDQINKEESYQPIVDYI 119
Cdd:COG3596   40 PVIALVGKTGAGKSSLINALFGAEVAEV--GVGRPCTR-EIQRYRLESDGLPG-LVLLDTPGLGEVNERDREYRELRELL 115

                 ..
gi 564397859 120 DN 121
Cdd:COG3596  116 PE 117
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
45-210 1.50e-06

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: 47.84  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  45 VGETGIGKSTLINTLFNTNFEELESSHFCPcvrLRAQTYELQESNVRLKLTIVNTVGFGDqinkeesyqpivdyidnqfE 124
Cdd:cd00882    3 VGRGGVGKSSLLNALLGGEVGEVSDVPGTT---RDPDVYVKELDKGKVKLVLVDTPGLDE-------------------F 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 125 AYLQEELKIKRALfnyhdSRIHVCLYFIAPTGH-SLRTLDLLTMKSLD-NKVNIIPLIAKADTISKSELQKFKMKLMSEL 202
Cdd:cd00882   61 GGLGREELARLLL-----RGADLILLVVDSTDReSEEDAKLLILRRLRkEGIPIILVGNKIDLLEEREVEELLRLEELAK 135

                 ....*...
gi 564397859 203 vINGVQIY 210
Cdd:cd00882  136 -ILGVPVF 142
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
242-385 4.65e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  242 KVGNKMVKARQYPWGIVQVENENHCDFVKLREMLICTNMEDLREQTHMRhyelyRRCKL----QEMGFIDIGPENKPLSL 317
Cdd:pfam17380 424 QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLelekEKRDRKRAEEQRRKILE 498
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  318 QETYEAKRHEFCGERQRK--EEQMKQMFVQRVKEKEAILKEAERELQAKFEHLKRIHQEERMKLEEKRRM 385
Cdd:pfam17380 499 KELEERKQAMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRL 568
PTZ00121 PTZ00121
MAEBL; Provisional
331-422 2.10e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  331 ERQRKEEQMKQMFVQRVKEKEAiLKEAERELQAKFEHLKRIHQEERMKLEEKRRMlEEESVAFAKKKATCELFPHQSFLA 410
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEE-LKKAEEENKIKAEEAKKEAEEDKKKAEEAKKD-EEEKKKIAHLKKEEEKKAEEIRKE 1776
                          90
                  ....*....|..
gi 564397859  411 SGSSIRRDKDRK 422
Cdd:PTZ00121 1777 KEAVIEEELDEE 1788
PTZ00121 PTZ00121
MAEBL; Provisional
281-389 2.29e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  281 EDLREQTHMRHYELYRRC-KLQEMGFIDIGPENKPLSLQETYEAKRHEFCGERQRKEEQMKQMFVQ-RVKEKEAI----- 353
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQlKKKEAEEKkkaee 1651
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 564397859  354 LKEAERELQAKFEHLKRIHQEERMKLEEKRRMLEEE 389
Cdd:PTZ00121 1652 LKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE 1687
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
333-389 3.70e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.10  E-value: 3.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564397859 333 QRKEEQMKQMFVQRVKEKEA-----ILKEAERELQAKFEHLKRIHQEE----RMKLEEKRRMLEEE 389
Cdd:cd16269  191 QALTEKEKEIEAERAKAEAAeqerkLLEEQQRELEQKLEDQERSYEEHlrqlKEKMEEERENLLKE 256
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
270-389 4.82e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.34  E-value: 4.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  270 KLREMLICTNMEDLREQTHMRHYELYRRcklqEMGFIDIGPEN-KPLSLQETYEAKRHEFcgERQRKEEQMKQMFVQRVK 348
Cdd:pfam17380 393 RVRQELEAARKVKILEEERQRKIQQQKV----EMEQIRAEQEEaRQREVRRLEEERAREM--ERVRLEEQERQQQVERLR 466
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 564397859  349 EKEAILKEAERELQAKFEHLKRIHQEERMKLEE--------------KRRMLEEE 389
Cdd:pfam17380 467 QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKeleerkqamieeerKRKLLEKE 521
Nup88 pfam10168
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ...
283-387 5.88e-03

Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.


Pssm-ID: 462975 [Multi-domain]  Cd Length: 713  Bit Score: 39.26  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859  283 LREQTHMRHY----ELYRRCK---------LQEMGfiDIGPENKplSLQETYE--AKRHEFCGERQRKEEQMKQMFVQRV 347
Cdd:pfam10168 544 FREEYLKKHDlareEIQKRVKllklqkeqqLQELQ--SLEEERK--SLSERAEklAEKYEEIKDKQEKLMRRCKKVLQRL 619
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 564397859  348 KEKEAILKEAERE-------LQAKFEHLKRIHQEERMKLEEKRRMLE 387
Cdd:pfam10168 620 NSQLPVLSDAEREmkkeletINEQLKHLANAIKQAKKKMNYQRYQIA 666
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
317-396 8.00e-03

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


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 36.69  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564397859 317 LQETYEAKRHEFCGERQRKEEQMKQmfvQRVKEKEAILKEAERELQAKFEH-LKRIHQEERMKLEEKRRMLEEESVAFAK 395
Cdd:COG0711   53 ALAEYEEKLAEARAEAAEIIAEARK---EAEAIAEEAKAEAEAEAERIIAQaEAEIEQERAKALAELRAEVADLAVAIAE 129

                 .
gi 564397859 396 K 396
Cdd:COG0711  130 K 130
PRK12704 PRK12704
phosphodiesterase; Provisional
331-401 8.89e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 8.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564397859 331 ERQRKEEQMKQMFVQRVKEKEAILKEAERELQAKFEHLKR----IHQEERmKLEEKRRMLEEESVAFAKKKATCE 401
Cdd:PRK12704  61 EAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRklelLEKREE-ELEKKEKELEQKQQELEKKEEELE 134
 
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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