NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|62955083|ref|NP_001017557|]
View 

septin 10 [Danio rerio]

Protein Classification

CDC_Septin and ATG16 domain-containing protein( domain architecture ID 11548867)

CDC_Septin and ATG16 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
39-307 2.65e-144

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: 411.94  E-value: 2.65e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  39 QGFCFNILCIGETGIGKSTLMDTLFNTNFENFESS-----HFEPKVKLRAQTYDLQESNVRLKLTVVNTVGFGDQMNKQE 113
Cdd:cd01850   1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPpapgeHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 114 SYQHIVDYIDTQFESYLQEELKIKRSlHNYHDSRIHACLYFIAPSGHSLKSLDLVTMKKLDSKVNIIPVIAKADTISKSE 193
Cdd:cd01850  81 CWKPIVDYIDDQFESYLREESRINRN-RRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 194 LHKFKIKIMSELVSNGVQIYQFPID--DETVAKINTAMNGHLPFAVVGSTEEVNIGNKMVKARQYPWGVVQVENENHCDF 271
Cdd:cd01850 160 LTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 62955083 272 VKLREMLICVNMEDLREQTHTRHYELYRRCKLEEMG 307
Cdd:cd01850 240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
ATG16 super family cl25514
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
309-393 1.43e-06

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


The actual alignment was detected with superfamily member pfam08614:

Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 48.39  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   309 KDTDPECKPVSLQQTYEAKRQEfLGELQRREEEMRQtfvqRVKEKEAELKDAERELQGKFEQLKRLHAdEKSKLEEKRRS 388
Cdd:pfam08614  44 KASPQSASIQSLEQLLAQLREE-LAELYRSRGELAQ----RLVDLNEELQELEKKLREDERRLAALEA-ERAQLEEKLKD 117

                  ....*
gi 62955083   389 LEEEM 393
Cdd:pfam08614 118 REEEL 122
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
39-307 2.65e-144

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: 411.94  E-value: 2.65e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  39 QGFCFNILCIGETGIGKSTLMDTLFNTNFENFESS-----HFEPKVKLRAQTYDLQESNVRLKLTVVNTVGFGDQMNKQE 113
Cdd:cd01850   1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPpapgeHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 114 SYQHIVDYIDTQFESYLQEELKIKRSlHNYHDSRIHACLYFIAPSGHSLKSLDLVTMKKLDSKVNIIPVIAKADTISKSE 193
Cdd:cd01850  81 CWKPIVDYIDDQFESYLREESRINRN-RRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 194 LHKFKIKIMSELVSNGVQIYQFPID--DETVAKINTAMNGHLPFAVVGSTEEVNIGNKMVKARQYPWGVVQVENENHCDF 271
Cdd:cd01850 160 LTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 62955083 272 VKLREMLICVNMEDLREQTHTRHYELYRRCKLEEMG 307
Cdd:cd01850 240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
40-305 2.58e-109

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: 323.10  E-value: 2.58e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083    40 GFCFNILCIGETGIGKSTLMDTLFNTNFENFE-----SSHFEPKVKLRAQTYDLQESNVRLKLTVVNTVGFGDQMNKQES 114
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARgipgpSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   115 YQHIVDYIDTQFESYLQEELKIKRslHNYHDSRIHACLYFIAPSGHSLKSLDLVTMKKLDSKVNIIPVIAKADTISKSEL 194
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNR--KSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   195 HKFKIKIMSELVSNGVQIYQFP---IDDETVAKINTAMNGHLPFAVVGSTEEVNIGNKMVKARQYPWGVVQVENENHCDF 271
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 62955083   272 VKLREMLICVNMEDLREQTHTRHYELYRRCKLEE 305
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
20-404 5.68e-104

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 313.11  E-value: 5.68e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  20 SGHVGFDSLPDQLVNKSTSQGFCFNILCIGETGIGKSTLMDTLFNT------NFENFESSHFEPKVKLRAQTYDLQESNV 93
Cdd:COG5019   1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTslvdetEIDDIRAEGTSPTLEIKITKAELEEDGF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  94 RLKLTVVNTVGFGDQMNKQESYQHIVDYIDTQFESYLQEELKIKRSlHNYHDSRIHACLYFIAPSGHSLKSLDLVTMKKL 173
Cdd:COG5019  81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRN-PKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 174 DSKVNIIPVIAKADTISKSELHKFKIKIMSELVSNGVQIYQ-FPIDDETVAKINTAM--NGHLPFAVVGSTEEVNIGNKM 250
Cdd:COG5019 160 SKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLEENQdlRSLIPFAIIGSNTEIENGGEQ 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 251 VKARQYPWGVVQVENENHCDFVKLREMLICVNMEDLREQTHTRHYELYRRCKLEemgfkdtdpeckpvSLQQTYEAKRQE 330
Cdd:COG5019 240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLS--------------GLKNSGEPSLKE 305
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62955083 331 FLGE-LQRREEEMRQTFVQRVKEKEAELKDAERELQGKFEQLkrlhadeKSKLEEKRRSLEEEMSVFSKRKAATE 404
Cdd:COG5019 306 IHEArLNEEERELKKKFTEKIREKEKRLEELEQNLIEERKEL-------NSKLEEIQKKLEDLEKRLEKLKSNKS 373
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
309-393 1.43e-06

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 48.39  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   309 KDTDPECKPVSLQQTYEAKRQEfLGELQRREEEMRQtfvqRVKEKEAELKDAERELQGKFEQLKRLHAdEKSKLEEKRRS 388
Cdd:pfam08614  44 KASPQSASIQSLEQLLAQLREE-LAELYRSRGELAQ----RLVDLNEELQELEKKLREDERRLAALEA-ERAQLEEKLKD 117

                  ....*
gi 62955083   389 LEEEM 393
Cdd:pfam08614 118 REEEL 122
PRK12704 PRK12704
phosphodiesterase; Provisional
325-409 5.96e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 5.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  325 EAKRQEFLGELQRREEEMRQTFVQRVKEKEAELKDAERELQGKFEQLKR---LHADEKSKLEEKRRSLEEEMSVFSKRKA 401
Cdd:PRK12704  52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRkleLLEKREEELEKKEKELEQKQQELEKKEE 131

                 ....*...
gi 62955083  402 ATELLQAQ 409
Cdd:PRK12704 132 ELEELIEE 139
PLN03118 PLN03118
Rab family protein; Provisional
35-104 1.94e-03

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 39.27  E-value: 1.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   35 KSTSQGFCFNILCIGETGIGKSTLMDTLFNTNFENfesshFEPKVKLRAQTYDLQESNVRLKLTVVNTVG 104
Cdd:PLN03118   7 QSSGYDLSFKILLIGDSGVGKSSLLVSFISSSVED-----LAPTIGVDFKIKQLTVGGKRLKLTIWDTAG 71
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
325-410 9.45e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 9.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 325 EAKRQEFLGELQRREEEMRQT------FVQRVKEKEAELKDAERELQgkfEQLKRLHADEKSKLEEKRRSLEEEMSVFSK 398
Cdd:COG1196 308 EERRRELEERLEELEEELAELeeeleeLEEELEELEEELEEAEEELE---EAEAELAEAEEALLEAEAELAEAEEELEEL 384
                        90
                ....*....|..
gi 62955083 399 RKAATELLQAQS 410
Cdd:COG1196 385 AEELLEALRAAA 396
 
Name Accession Description Interval E-value
CDC_Septin cd01850
CDC/Septin GTPase family; Septins are a conserved family of GTP-binding proteins associated ...
39-307 2.65e-144

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: 411.94  E-value: 2.65e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  39 QGFCFNILCIGETGIGKSTLMDTLFNTNFENFESS-----HFEPKVKLRAQTYDLQESNVRLKLTVVNTVGFGDQMNKQE 113
Cdd:cd01850   1 RGFQFNIMVVGESGLGKSTFINTLFGTKLYPSKYPpapgeHITKTVEIKISKAELEENGVKLKLTVIDTPGFGDNINNSD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 114 SYQHIVDYIDTQFESYLQEELKIKRSlHNYHDSRIHACLYFIAPSGHSLKSLDLVTMKKLDSKVNIIPVIAKADTISKSE 193
Cdd:cd01850  81 CWKPIVDYIDDQFESYLREESRINRN-RRIPDTRVHCCLYFIPPTGHGLKPLDIEFMKKLSKKVNIIPVIAKADTLTPEE 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 194 LHKFKIKIMSELVSNGVQIYQFPID--DETVAKINTAMNGHLPFAVVGSTEEVNIGNKMVKARQYPWGVVQVENENHCDF 271
Cdd:cd01850 160 LTEFKKRIMEDIEENNIKIYKFPEDeeDEEEIEENKKLKSLIPFAIVGSNEEVEVNGKKVRGRKYPWGVVEVENEEHCDF 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 62955083 272 VKLREMLICVNMEDLREQTHTRHYELYRRCKLEEMG 307
Cdd:cd01850 240 VKLRNLLIRTHLQDLKETTHNVHYENYRSEKLEALK 275
Septin pfam00735
Septin; Members of this family include CDC3, CDC10, CDC11 and CDC12/Septin. Members of this ...
40-305 2.58e-109

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: 323.10  E-value: 2.58e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083    40 GFCFNILCIGETGIGKSTLMDTLFNTNFENFE-----SSHFEPKVKLRAQTYDLQESNVRLKLTVVNTVGFGDQMNKQES 114
Cdd:pfam00735   1 GFDFTLMVVGESGLGKTTFINTLFLTDLYRARgipgpSEKIKKTVEIKAYTVEIEEDGVKLNLTVIDTPGFGDAIDNSNC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   115 YQHIVDYIDTQFESYLQEELKIKRslHNYHDSRIHACLYFIAPSGHSLKSLDLVTMKKLDSKVNIIPVIAKADTISKSEL 194
Cdd:pfam00735  81 WRPIVEYIDEQYEQYLRDESGLNR--KSIKDNRVHCCLYFISPTGHGLKPLDVEFMKKLSEKVNIIPVIAKADTLTPDEL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   195 HKFKIKIMSELVSNGVQIYQFP---IDDETVAKINTAMNGHLPFAVVGSTEEVNIGNKMVKARQYPWGVVQVENENHCDF 271
Cdd:pfam00735 159 QRFKKRIREEIERQNIPIYHFPdeeSDEDEEKELNEQLKSSIPFAIVGSNTVIENDGEKVRGRKYPWGVVEVENPSHCDF 238
                         250       260       270
                  ....*....|....*....|....*....|....
gi 62955083   272 VKLREMLICVNMEDLREQTHTRHYELYRRCKLEE 305
Cdd:pfam00735 239 LKLRNMLIRTHLQDLKEVTHELHYETYRSEKLSA 272
CDC3 COG5019
Septin family protein [Cell cycle control, cell division, chromosome partitioning, ...
20-404 5.68e-104

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


Pssm-ID: 227352 [Multi-domain]  Cd Length: 373  Bit Score: 313.11  E-value: 5.68e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  20 SGHVGFDSLPDQLVNKSTSQGFCFNILCIGETGIGKSTLMDTLFNT------NFENFESSHFEPKVKLRAQTYDLQESNV 93
Cdd:COG5019   1 NGYVGISNLPNQRHRKLSKKGIDFTIMVVGESGLGKTTFINTLFGTslvdetEIDDIRAEGTSPTLEIKITKAELEEDGF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  94 RLKLTVVNTVGFGDQMNKQESYQHIVDYIDTQFESYLQEELKIKRSlHNYHDSRIHACLYFIAPSGHSLKSLDLVTMKKL 173
Cdd:COG5019  81 HLNLTVIDTPGFGDFIDNSKCWEPIVDYIDDQFDQYLDEEQKIKRN-PKFKDTRVHACLYFIRPTGHGLKPLDIEAMKRL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 174 DSKVNIIPVIAKADTISKSELHKFKIKIMSELVSNGVQIYQ-FPIDDETVAKINTAM--NGHLPFAVVGSTEEVNIGNKM 250
Cdd:COG5019 160 SKRVNLIPVIAKADTLTDDELAEFKERIREDLEQYNIPVFDpYDPEDDEDESLEENQdlRSLIPFAIIGSNTEIENGGEQ 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 251 VKARQYPWGVVQVENENHCDFVKLREMLICVNMEDLREQTHTRHYELYRRCKLEemgfkdtdpeckpvSLQQTYEAKRQE 330
Cdd:COG5019 240 VRGRKYPWGVVEIDDEEHSDFKKLRNLLIRTHLQELKETTENLLYENYRTEKLS--------------GLKNSGEPSLKE 305
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62955083 331 FLGE-LQRREEEMRQTFVQRVKEKEAELKDAERELQGKFEQLkrlhadeKSKLEEKRRSLEEEMSVFSKRKAATE 404
Cdd:COG5019 306 IHEArLNEEERELKKKFTEKIREKEKRLEELEQNLIEERKEL-------NSKLEEIQKKLEDLEKRLEKLKSNKS 373
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
309-393 1.43e-06

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 48.39  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   309 KDTDPECKPVSLQQTYEAKRQEfLGELQRREEEMRQtfvqRVKEKEAELKDAERELQGKFEQLKRLHAdEKSKLEEKRRS 388
Cdd:pfam08614  44 KASPQSASIQSLEQLLAQLREE-LAELYRSRGELAQ----RLVDLNEELQELEKKLREDERRLAALEA-ERAQLEEKLKD 117

                  ....*
gi 62955083   389 LEEEM 393
Cdd:pfam08614 118 REEEL 122
YeeP COG3596
Predicted GTPase [General function prediction only];
43-124 2.66e-06

Predicted GTPase [General function prediction only];


Pssm-ID: 442815 [Multi-domain]  Cd Length: 318  Bit Score: 48.99  E-value: 2.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  43 FNILCIGETGIGKSTLMDTLFNTNFEnfESSHFEPkVKLRAQTYDLQESNVRLkLTVVNTVGFGDQMNKQESYQHIVDYI 122
Cdd:COG3596  40 PVIALVGKTGAGKSSLINALFGAEVA--EVGVGRP-CTREIQRYRLESDGLPG-LVLLDTPGLGEVNERDREYRELRELL 115

                ..
gi 62955083 123 DT 124
Cdd:COG3596 116 PE 117
PRK12704 PRK12704
phosphodiesterase; Provisional
325-409 5.96e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.24  E-value: 5.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  325 EAKRQEFLGELQRREEEMRQTFVQRVKEKEAELKDAERELQGKFEQLKR---LHADEKSKLEEKRRSLEEEMSVFSKRKA 401
Cdd:PRK12704  52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRkleLLEKREEELEKKEKELEQKQQELEKKEE 131

                 ....*...
gi 62955083  402 ATELLQAQ 409
Cdd:PRK12704 132 ELEELIEE 139
PTZ00121 PTZ00121
MAEBL; Provisional
273-395 1.14e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   273 KLREMLICVNMEDLREQTHTRHYELYRRCKLEEMGFKDTDPECKPVSLQQTYEAKRQEfLGELQRREEEMRQtfVQRVKE 352
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA-AEALKKEAEEAKK--AEELKK 1709
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 62955083   353 KEAE-------LKDAERELQGKFEQLKRLHADEKSKLEEKRRSLEEEMSV 395
Cdd:PTZ00121 1710 KEAEekkkaeeLKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
252-405 6.54e-05

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: 45.11  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   252 KARQYPWGVVQVENENHCDFVKLREMLICVNMEDLREQTHTRhyelyRRCKLE---EMGFKDTDPECKPVSLQQTYEAKR 328
Cdd:pfam17380 431 EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEER-----KRKKLElekEKRDRKRAEEQRRKILEKELEERK 505
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   329 QEFLGELQRR---EEEM--RQTFV----QRVKEKEAELKDAERELQGKFEQLKRLHADEKSKLEEKRRSLEEEMSVFSKR 399
Cdd:pfam17380 506 QAMIEEERKRkllEKEMeeRQKAIyeeeRRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESE 585

                  ....*.
gi 62955083   400 KAATEL 405
Cdd:pfam17380 586 KARAEY 591
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
48-208 1.93e-04

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: 41.67  E-value: 1.93e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  48 IGETGIGKSTLMDTLFNTNFenFESSHfEPKVKLRAQTYDLQESNVRLKLTVVNTVGFGDqmnkqesyqhivdyidtqfE 127
Cdd:cd00882   3 VGRGGVGKSSLLNALLGGEV--GEVSD-VPGTTRDPDVYVKELDKGKVKLVLVDTPGLDE-------------------F 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 128 SYLQEELKIKRSLhnyhdSRIHACLYFIAPSGH-SLKSLDLVTMKKLDS-KVNIIPVIAKADTISKSELHKFKIKIMSEL 205
Cdd:cd00882  61 GGLGREELARLLL-----RGADLILLVVDSTDReSEEDAKLLILRRLRKeGIPIILVGNKIDLLEEREVEELLRLEELAK 135

                ...
gi 62955083 206 VSN 208
Cdd:cd00882 136 ILG 138
PTZ00121 PTZ00121
MAEBL; Provisional
274-421 2.60e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   274 LREMLICVNMEDLREQTHTRHYELYRRCKLEEMGfKDTDPECKPVSLQQTYEAKRQEFLGELQRREEEMRQTFVQRVKE- 352
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK-KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEe 1658
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62955083   353 ---KEAELKDAERELQGKFEQLKRLHADEKSKLEEKRRSLEEEMSVFS-KRKAATELLQAQSFNTSTNNKKDK 421
Cdd:PTZ00121 1659 nkiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElKKKEAEEKKKAEELKKAEEENKIK 1731
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
321-404 8.15e-04

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: 41.70  E-value: 8.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083    321 QQTYEAKRQEFLGELQRREEEMRQTFVQRVKEKEAELKDAERELQGKFEQLKRLHAD-EKSK--LEEKRRSLEEEMSVFS 397
Cdd:pfam01576  318 QQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANlEKAKqaLESENAELQAELRTLQ 397

                   ....*..
gi 62955083    398 KRKAATE 404
Cdd:pfam01576  398 QAKQDSE 404
PTZ00121 PTZ00121
MAEBL; Provisional
262-423 9.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   262 QVENENHCDFVKLREMLICVNMEDLREQTHTRhyelyrrCKLEEMgfKDTDPECKPVSLQQTYEAKRQEFLGELQRREEE 341
Cdd:PTZ00121 1588 KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK-------IKAEEL--KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEE 1658
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   342 MRQTFVQRVKEKEA------ELKDAERELQGKFEQLKRlHADEKSKLEEKRRSLEEEMSVFSKRKAATELLQAQSFNTST 415
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEdkkkaeEAKKAEEDEKKAAEALKK-EAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKK 1737

                  ....*...
gi 62955083   416 NNKKDKDR 423
Cdd:PTZ00121 1738 EAEEDKKK 1745
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
334-409 9.94e-04

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 38.57  E-value: 9.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62955083   334 ELQRREEEMRQTFVQRVKEKEAElkdAERELQGKFEQLKRLHADEKSKLEEKRRSLEEEmsvfSKRKAATELLQAQ 409
Cdd:pfam16999  16 ALDQQIEAARKEAEREVEAAEAE---AARILREAEAKAKALQAEYRQELAAETARIREE----ARARAEAEAQAVR 84
PRK14475 PRK14475
F0F1 ATP synthase subunit B; Provisional
324-410 1.04e-03

F0F1 ATP synthase subunit B; Provisional


Pssm-ID: 184697 [Multi-domain]  Cd Length: 167  Bit Score: 39.54  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083  324 YEAKRQEFLGELQRREEEMRQTFVQRVKEKEAELKDAERELQGKFEQLKRLHADEKSKLEE--KRRSleeEMsvfSKRKA 401
Cdd:PRK14475  42 YAAKIQAELDEAQRLREEAQALLADVKAEREEAERQAAAMLAAAKADARRMEAEAKEKLEEqiKRRA---EM---AERKI 115

                 ....*....
gi 62955083  402 ATELLQAQS 410
Cdd:PRK14475 116 AQAEAQAAA 124
PTZ00121 PTZ00121
MAEBL; Provisional
284-422 1.40e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   284 EDLREQTHTRHYELYRRCKLEEMGFKDTDPECKPVSLQQTYEAKRQEFLGELQRREEEMRQTFVQRVKE---KEAELKDA 360
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEakiKAEELKKA 1628
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62955083   361 ErELQGKFEQLKRLHADEKSKLEEKRRSlEEEMSVFS---KRKAATELLQAQSFNTSTNNKKDKD 422
Cdd:PTZ00121 1629 E-EEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAaeeAKKAEEDKKKAEEAKKAEEDEKKAA 1691
PLN03118 PLN03118
Rab family protein; Provisional
35-104 1.94e-03

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 39.27  E-value: 1.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   35 KSTSQGFCFNILCIGETGIGKSTLMDTLFNTNFENfesshFEPKVKLRAQTYDLQESNVRLKLTVVNTVG 104
Cdd:PLN03118   7 QSSGYDLSFKILLIGDSGVGKSSLLVSFISSSVED-----LAPTIGVDFKIKQLTVGGKRLKLTIWDTAG 71
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
325-392 4.31e-03

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 37.72  E-value: 4.31e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62955083   325 EAKRQEFLGELQRREEEMRQTFVQRV-----KEKEAELKDAER---ELQGKFEQLKRLHADEKSKLEEKRRSLEEE 392
Cdd:pfam15346  29 EKRKDEIEAEVERRVEEARKIMEKQVleeleREREAELEEERRkeeEERKKREELERILEENNRKIEEAQRKEAEE 104
PTZ00121 PTZ00121
MAEBL; Provisional
302-424 6.41e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083   302 KLEEMGFKDTDPECKPVSLQQTYEAKRQEflGELQRREEEMRQTfVQRVKEKEAELKDAErELQGKFEQLKRlhADE-KS 380
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEEKKKA--DEAKKKAEEDKKK-ADELKKAAAAKKKAD-EAKKKAEEKKK--ADEaKK 1438
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 62955083   381 KLEEKRRSLEEEMSVFSKRKAATELLQAQSFNTSTNNKKDKDRK 424
Cdd:PTZ00121 1439 KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
338-407 7.82e-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: 36.82  E-value: 7.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62955083   338 REEEMRQTFVQRVKEKEAELKDAERELQGKFEQL----KRLHADEKSKLEEKRRSLEEEMSVFSKRKaaTELLQ 407
Cdd:pfam09744  68 REKALRKRAEEELEEIEDQWEQETKDLLSQVESLeeenRRLEADHVSRLEEKEAELKKEYSKLHERE--TEVLR 139
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
325-410 9.45e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 9.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955083 325 EAKRQEFLGELQRREEEMRQT------FVQRVKEKEAELKDAERELQgkfEQLKRLHADEKSKLEEKRRSLEEEMSVFSK 398
Cdd:COG1196 308 EERRRELEERLEELEEELAELeeeleeLEEELEELEEELEEAEEELE---EAEAELAEAEEALLEAEAELAEAEEELEEL 384
                        90
                ....*....|..
gi 62955083 399 RKAATELLQAQS 410
Cdd:COG1196 385 AEELLEALRAAA 396
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH