NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2217268679|ref|XP_047279986|]
View 

protein misato homolog 1 isoform X4 [Homo sapiens]

Protein Classification

misato family protein( domain architecture ID 10149475)

misato family protein similar to human protein misato homolog 1 that regulates mitochondrial distribution and morphology, and is required for mitochondrial fusion and mitochondrial network formation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
 88-457 2.28e-146

Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family of GTPases and is localized to the the outer membrane of mitochondria. It has a role in mitochondrial fusion and in mitochondrial distribution and morphology. Mutations in its Drosophila homolog (misato) lead to irregular chromosome segregation during mitosis. Deletion of the budding yeast homolog DML1 is lethal and unregulate expression of DML1 leads to mitochondrial dispersion and abnormalities in cell morphology. The Misato/DML1 protein family is conserved from yeast to human, but its exact function is still unknown.


:

Pssm-ID: 276964 [Multi-domain]  Cd Length: 539  Bit Score: 428.66  E-value: 2.28e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679  88 SPLPTATTPKPLIPTEASIRVWSDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDRLHFYVEEC 167
Cdd:cd06060   125 ESQSTAEDGDKVYLLEESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEEC 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 168 DYLQGFQILCDLHDGFSGVGAKAAELLQDEYSGRGIITWGLLPGP----------------------------------- 212
Cdd:cd06060   205 DSLQGFQILVDTDDGFGGVAAKLLENLRDEYGKKSILTPGLSPASppdpdsqrrikrllndalslsslsehsslfvplsl 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 213 --------------YHRGATLPFHCSAILATALDTVTVPYRLCSSPVSMVHLADMLSFCGKKVVTAGAIIPFPLAPGQSL 278
Cdd:cd06060   285 psllwrkpgwprtfPHLDYSSPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSL 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 279 PDSLMQFGGATPWTPlsacGEPSGTRCFAQSVVLRGIDRACHTSQltpgTPPPSALHACTTGEEILAQYLQQQQPGVMSS 358
Cdd:cd06060   365 LDSLQDLLGDLSLTP----SCQNETDVFAQSVVLRGIPESRLKSP----LQPRSPASRCSSVEEVLEGYLQCTFPGSSSA 436

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 359 SHLLLTPCRVAPPYPHLFSSC-SPPGMVLDGSPKGA-AVESIPVFGALCSSSSLHQTLEALARDLTKLDLRRWASFMDAG 436
Cdd:cd06060   437 VTTLPQPLPVPTPFPSIFSPSlGRKGFLLDDSRPASlDVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGG 516

                         410       420
                  ....*....|....*....|..
gi 2217268679 437 -VEHDDVAELLQELQSLAQCYQ 457
Cdd:cd06060   517 gLERDEFKESLEELLSLADCYG 538
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
 88-457 2.28e-146

Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family of GTPases and is localized to the the outer membrane of mitochondria. It has a role in mitochondrial fusion and in mitochondrial distribution and morphology. Mutations in its Drosophila homolog (misato) lead to irregular chromosome segregation during mitosis. Deletion of the budding yeast homolog DML1 is lethal and unregulate expression of DML1 leads to mitochondrial dispersion and abnormalities in cell morphology. The Misato/DML1 protein family is conserved from yeast to human, but its exact function is still unknown.


Pssm-ID: 276964 [Multi-domain]  Cd Length: 539  Bit Score: 428.66  E-value: 2.28e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679  88 SPLPTATTPKPLIPTEASIRVWSDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDRLHFYVEEC 167
Cdd:cd06060   125 ESQSTAEDGDKVYLLEESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEEC 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 168 DYLQGFQILCDLHDGFSGVGAKAAELLQDEYSGRGIITWGLLPGP----------------------------------- 212
Cdd:cd06060   205 DSLQGFQILVDTDDGFGGVAAKLLENLRDEYGKKSILTPGLSPASppdpdsqrrikrllndalslsslsehsslfvplsl 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 213 --------------YHRGATLPFHCSAILATALDTVTVPYRLCSSPVSMVHLADMLSFCGKKVVTAGAIIPFPLAPGQSL 278
Cdd:cd06060   285 psllwrkpgwprtfPHLDYSSPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSL 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 279 PDSLMQFGGATPWTPlsacGEPSGTRCFAQSVVLRGIDRACHTSQltpgTPPPSALHACTTGEEILAQYLQQQQPGVMSS 358
Cdd:cd06060   365 LDSLQDLLGDLSLTP----SCQNETDVFAQSVVLRGIPESRLKSP----LQPRSPASRCSSVEEVLEGYLQCTFPGSSSA 436

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 359 SHLLLTPCRVAPPYPHLFSSC-SPPGMVLDGSPKGA-AVESIPVFGALCSSSSLHQTLEALARDLTKLDLRRWASFMDAG 436
Cdd:cd06060   437 VTTLPQPLPVPTPFPSIFSPSlGRKGFLLDDSRPASlDVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGG 516

                         410       420
                  ....*....|....*....|..
gi 2217268679 437 -VEHDDVAELLQELQSLAQCYQ 457
Cdd:cd06060   517 gLERDEFKESLEELLSLADCYG 538
Tubulin_3 pfam14881
Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ...
 101-240 1.19e-21

Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Misato from Drosophila and Dml1p from fungi are descendants of an ancestral tubulin-like protein, and exhibit regions with similarity to members of a GTPase family that includes eukaryotic tubulin and prokaryotic FtsZ. Dml1p and Misato have been co-opted into a role in mtDNA inheritance in yeast, and into a cell division-related mechanism in flies, respectively. Dml1p might additionally function in the partitioning of the mitochondrial organelle itself, or in the segregation of chromosomes, thereby explaining its essential requirement. This domain subject to extensive post-translational modifications.


Pssm-ID: 434281 [Multi-domain]  Cd Length: 180  Bit Score: 92.05  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 101 PTEASIRVWSDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDR-LHFYVEECDYLQGFQILCDL 179
Cdd:pfam14881   4 LTTSTVRYWSDFNRVFYHPRSIVQLNEYELNSQLMPFEDWSVGEELFRELDKEHDLLDRdLRPFAEECDQLQGLQVFTGS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 180 HDGFSGVGAKAAELLQDEYSGRGII-TWGL-LPGPYHRGATL----------------------------------PFHC 223
Cdd:pfam14881  84 DDAWGGFAARYLERLRDEYGKKSIIwVWALqDPLKRIRRTKRerrlrlankarslqslspqaslyvpiatlsdgqsEWHT 163

                         170
                  ....*....|....*..
gi 2217268679 224 SAILATALDTVTVPYRL 240
Cdd:pfam14881 164 SALLSSAIESATLPSRL 180
PTZ00387 PTZ00387
epsilon tubulin; Provisional
 150-198 4.99e-04

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 42.40  E-value: 4.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217268679 150 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEY 198
Cdd:PTZ00387  111 DKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTgSGLGTRILGMLEDEF 160
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
 88-457 2.28e-146

Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family of GTPases and is localized to the the outer membrane of mitochondria. It has a role in mitochondrial fusion and in mitochondrial distribution and morphology. Mutations in its Drosophila homolog (misato) lead to irregular chromosome segregation during mitosis. Deletion of the budding yeast homolog DML1 is lethal and unregulate expression of DML1 leads to mitochondrial dispersion and abnormalities in cell morphology. The Misato/DML1 protein family is conserved from yeast to human, but its exact function is still unknown.


Pssm-ID: 276964 [Multi-domain]  Cd Length: 539  Bit Score: 428.66  E-value: 2.28e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679  88 SPLPTATTPKPLIPTEASIRVWSDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDRLHFYVEEC 167
Cdd:cd06060   125 ESQSTAEDGDKVYLLEESVRVWSDYLRVYYHPRSINVLNEYQHDSEFNPFDNFSQGEELFSDLEELEEFEDRLRFFVEEC 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 168 DYLQGFQILCDLHDGFSGVGAKAAELLQDEYSGRGIITWGLLPGP----------------------------------- 212
Cdd:cd06060   205 DSLQGFQILVDTDDGFGGVAAKLLENLRDEYGKKSILTPGLSPASppdpdsqrrikrllndalslsslsehsslfvplsl 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 213 --------------YHRGATLPFHCSAILATALDTVTVPYRLCSSPVSMVHLADMLSFCGKKVVTAGAIIPFPLAPGQSL 278
Cdd:cd06060   285 psllwrkpgwprtfPHLDYSSPYHTSAVLAAALDTATLPYRLKSSSVSMSDLCSSLTFSGRKVAALSLALPFPLLLGSSL 364

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 279 PDSLMQFGGATPWTPlsacGEPSGTRCFAQSVVLRGIDRACHTSQltpgTPPPSALHACTTGEEILAQYLQQQQPGVMSS 358
Cdd:cd06060   365 LDSLQDLLGDLSLTP----SCQNETDVFAQSVVLRGIPESRLKSP----LQPRSPASRCSSVEEVLEGYLQCTFPGSSSA 436

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 359 SHLLLTPCRVAPPYPHLFSSC-SPPGMVLDGSPKGA-AVESIPVFGALCSSSSLHQTLEALARDLTKLDLRRWASFMDAG 436
Cdd:cd06060   437 VTTLPQPLPVPTPFPSIFSPSlGRKGFLLDDSRPASlDVESVPVLASLQSSSALGPLLEELASEVEKLGLRKLHEFLGGG 516

                         410       420
                  ....*....|....*....|..
gi 2217268679 437 -VEHDDVAELLQELQSLAQCYQ 457
Cdd:cd06060   517 gLERDEFKESLEELLSLADCYG 538
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
 99-407 1.37e-82

Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, gamma-, delta-, epsilon, and zeta-tubulins as well as FtsZ and CetZ, all of which are involved in polymer formation. Tubulin is the major component of microtubules, but also exists as a heterodimer and as a curved oligomer. Microtubules exist in all eukaryotic cells and are responsible for many functions, including cellular transport, cell motility, and mitosis. FtsZ forms a ring-shaped septum at the site of bacterial cell division, which is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria, archaea, and chloroplasts. A recent study found that CetZ proteins, formerly annotated FtsZ type 2, are not required for cell division, whereas FtsZ proteins play an important role. Instead, CetZ proteins are shown to be involved in controlling archaeal cell shape dynamics. The results from inactivation studies of CetZ proteins in Haloferax volcanii suggest that CetZ1 is essential for normal swimming motility and rod-cell development.


Pssm-ID: 276954 [Multi-domain]  Cd Length: 332  Bit Score: 258.11  E-value: 1.37e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679  99 LIPTEAS--IRVWSDFLRVHLHPRSICMIQKYnhdgeAGRLEAFGQGESVLkEPKYQEELEDRLHFYVEECDYLQGFQIL 176
Cdd:cd00286    24 LVDLEPAvlDELLSGPLRQLFHPENIILIQKY-----HGAGNNWAKGHSVA-GEEYQEEILDAIRKEVEECDELQGFFIT 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 177 CDLHDG-FSGVGAKAAELLQDEYSGRGIITWGLLPGPYHRG--------------------------------------- 216
Cdd:cd00286    98 HSLGGGtGSGLGPLLAERLKDEYPNRLVVTFSILPGPDEGVivypynaaltlktltehadclllvdnealydicprplhi 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 217 -ATLPFHCSAILATALDTVTVPYRLCSSPVSMVHLadmlsfcgkkvvtaGAIIPFPLAPGQSLPDSLMQFGGATPWTPLS 295
Cdd:cd00286   178 dAPAYDHINELVAQRLGSLTEALRFEGSLNVDLRE--------------LAENLVPLPRGHFLMLGYAPLDSATSATPRS 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 296 ACGEPSGTRCFAQSVVLRGidrachtsqltpgtpppsalHACTTGEEILAQYLQQQQPGvMSSSHLLLTPCRVAPPYPHL 375
Cdd:cd00286   244 LRVKELTRRAFLPANLLVG--------------------CDPDHGEAIAALLVIRGPPD-LSSKEVERAIARVKETLGHL 302

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2217268679 376 FsSCSPPGMVLDGSPKGAAvESIPVFGALCSS 407
Cdd:cd00286   303 F-SWSPAGVKTGISPKPPA-EGEVSVLALLNS 332
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
 113-458 1.97e-73

The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins. Also included in this group is the mitochondrial Misato/DML1 protein family, involved in mitochondrial fusion and in mitochondrial distribution and morphology.


Pssm-ID: 276963 [Multi-domain]  Cd Length: 387  Bit Score: 236.33  E-value: 1.97e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 113 LRVHLHPRSICMIQKynhdgeaGRLEAFGQGESVLKePKYQEELEDRLHFYVEECDYLQGFQILCDLHDG-FSGVGAKAA 191
Cdd:cd06059    42 LGQLFDPNQFVTGVS-------GAGNNWAVGYYVYG-PKYIESILDRIRKQVEKCDSLQGFFILHSLGGGtGSGLGSYLL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 192 ELLQDEYSGRGIITWGLLPGPYHRG--------------------ATLPF------------------------HCSAIL 227
Cdd:cd06059   114 ELLEDEYPKVYRFTFSVFPSPDDDNvitspynsvlalnhltehadCVLPIdnealydicnrqpatldidfppfdDMNNLV 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 228 ATALDTVTVPYRLCSSpvSMVHLADMLSfcgkkvvtagAIIPFPLapGQSLPDSLMQFGGATPWTPLSACGEPSGTRCFA 307
Cdd:cd06059   194 AQLLSSLTSSLRFEGS--LNVDLNEITT----------NLVPFPR--LHFLLPSLSPLTSANDVTLEPLTLDQLFSDLFS 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 308 QSVVLRGIDrachtsqltpgtpppsalhaCTTGEEILAQYLQQQQpgVMSSSHLLLTPCRVAPPYPHLfsSCSPPGMVLD 387
Cdd:cd06059   260 KDNQLVGCD--------------------PRHGTYLACALLLRGK--VFSLSDVRRNIDRIKPKLKFI--SWNPDGFKVG 315

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217268679 388 GSPKgAAVESIPVFGALCSSSSLHQTLEALARDLTKLDLRRWASFMDAGV--EHDDVAELLQELQSLAQCYQG 458
Cdd:cd06059   316 LCSV-PPVGQKYSLLFLSNNTSIASTFERLIERFDKLYKRKAFLHHYTGEgmEEGDFSEARESLANLIQEYQE 387
Tubulin_3 pfam14881
Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ...
 101-240 1.19e-21

Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Misato from Drosophila and Dml1p from fungi are descendants of an ancestral tubulin-like protein, and exhibit regions with similarity to members of a GTPase family that includes eukaryotic tubulin and prokaryotic FtsZ. Dml1p and Misato have been co-opted into a role in mtDNA inheritance in yeast, and into a cell division-related mechanism in flies, respectively. Dml1p might additionally function in the partitioning of the mitochondrial organelle itself, or in the segregation of chromosomes, thereby explaining its essential requirement. This domain subject to extensive post-translational modifications.


Pssm-ID: 434281 [Multi-domain]  Cd Length: 180  Bit Score: 92.05  E-value: 1.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 101 PTEASIRVWSDFLRVHLHPRSICMIQKYNHDGEAGRLEAFGQGESVLKEPKYQEELEDR-LHFYVEECDYLQGFQILCDL 179
Cdd:pfam14881   4 LTTSTVRYWSDFNRVFYHPRSIVQLNEYELNSQLMPFEDWSVGEELFRELDKEHDLLDRdLRPFAEECDQLQGLQVFTGS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 180 HDGFSGVGAKAAELLQDEYSGRGII-TWGL-LPGPYHRGATL----------------------------------PFHC 223
Cdd:pfam14881  84 DDAWGGFAARYLERLRDEYGKKSIIwVWALqDPLKRIRRTKRerrlrlankarslqslspqaslyvpiatlsdgqsEWHT 163

                         170
                  ....*....|....*..
gi 2217268679 224 SAILATALDTVTVPYRL 240
Cdd:pfam14881 164 SALLSSAIESATLPSRL 180
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
 150-198 6.28e-06

The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The epsilon-tubulins which are widespread but not ubiquitous among eukaryotes play a role in basal body/centriole morphogenesis.


Pssm-ID: 276959 [Multi-domain]  Cd Length: 449  Bit Score: 48.39  E-value: 6.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217268679 150 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEY 198
Cdd:cd02190   116 PQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTgSGLGSYILELLEDEF 165
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
 111-210 1.43e-05

Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. Members of this family are involved in polymer formation. FtsZ is the polymer-forming protein of bacterial cell division. It is part of a ring in the middle of the dividing cell that is required for constriction of cell membrane and cell envelope to yield two daughter cells. FtsZ and tubulin are GTPases. FtsZ can polymerize into tubes, sheets, and rings in vitro and is ubiquitous in eubacteria and archaea. Tubulin is the major component of microtubules.


Pssm-ID: 459669 [Multi-domain]  Cd Length: 190  Bit Score: 45.67  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 111 DFLRVHLHPRSICMIQKynhdgEAGRLEAFGQGEsvlKEPKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAK 189
Cdd:pfam00091  58 NEIKAGFNPNKILLGKE-----GTGGNGAGGYPE---IGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTgSGAAPV 129

                          90       100
                  ....*....|....*....|.
gi 2217268679 190 AAELLQDEYSGRGIITWGLLP 210
Cdd:pfam00091 130 IAEILKELYPGALTVAVVTFP 150
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 150-212 1.07e-04

The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276956 [Multi-domain]  Cd Length: 425  Bit Score: 44.48  E-value: 1.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217268679 150 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLPGP 212
Cdd:cd02187   109 AELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTgSGLGTLLLSKLREEYPDRIMSTFSVLPSP 172
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
 140-198 1.43e-04

The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. Delta-tubulin plays an essential role in forming the triplet microtubules of centrioles and basal bodies.


Pssm-ID: 276958 [Multi-domain]  Cd Length: 433  Bit Score: 44.18  E-value: 1.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 140 FGQGESVLkepkyqEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEY 198
Cdd:cd02189   100 YVHGPSLL------EDILEALRREAERCDRLSGFLVLHSLAGGTgSGLGSRVTELLRDEY 153
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
 151-212 4.08e-04

The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, beta-, gamma-, delta-, and epsilon-tubulins and a sixth family (zeta-tubulin) which is present only in kinetoplastid protozoa. The alpha- and beta-tubulins are the major components of microtubules, while gamma-tubulin plays a major role in the nucleation of microtubule assembly. The delta- and epsilon-tubulins are widespread but unlike the alpha, beta, and gamma-tubulins they are not ubiquitous among eukaryotes. The alpha/beta-tubulin heterodimer is the structural subunit of microtubules. The alpha- and beta-tubulins share 40% amino-acid sequence identity, exist in several isotype forms, and undergo a variety of posttranslational modifications. The structures of alpha- and beta-tubulin are basically identical: each monomer is formed by a core of two beta-sheets surrounded by alpha-helices. The monomer structure is very compact, but can be divided into three regions based on function: the amino-terminal nucleotide-binding region, an intermediate taxol-binding region and the carboxy-terminal region which probably constitutes the binding surface for motor proteins.


Pssm-ID: 276955 [Multi-domain]  Cd Length: 434  Bit Score: 42.53  E-value: 4.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217268679 151 KYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLPGP 212
Cdd:cd02186   112 EIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTgSGLTSLLLERLSVDYGKKSKLEFSIYPSP 174
PTZ00387 PTZ00387
epsilon tubulin; Provisional
 150-198 4.99e-04

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 42.40  E-value: 4.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2217268679 150 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEY 198
Cdd:PTZ00387  111 DKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTgSGLGTRILGMLEDEF 160
PTZ00010 PTZ00010
tubulin beta chain; Provisional
 150-212 2.49e-03

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 40.14  E-value: 2.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217268679 150 PKYQEELEDRLHFYVEECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLPGP 212
Cdd:PTZ00010  110 AELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTgSGMGTLLISKLREEYPDRIMMTFSVFPSP 173
PLN00220 PLN00220
tubulin beta chain; Provisional
 165-252 3.42e-03

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 39.81  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 165 EECDYLQGFQILCDLHDGF-SGVGAKAAELLQDEYSGRGIITWGLLPGPyhrgatlpfhcsailaTALDTVTVPYRLCSS 243
Cdd:PLN00220  125 ENCDCLQGFQVCHSLGGGTgSGMGTLLISKIREEYPDRMMLTFSVFPSP----------------KVSDTVVEPYNATLS 188


                  ....*....
gi 2217268679 244 PVSMVHLAD 252
Cdd:PLN00220  189 VHQLVENAD 197
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
 117-210 5.40e-03

The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of tubulin superfamily. Gamma is a low abundance protein present within the cells in both various types of microtubule-organizing centers and cytoplasmic protein complexes. Gamma-tubulin recruits the alpha/beta-tubulin dimers that form the minus ends of microtubules and is thought to be involved in microtubule nucleation and capping.


Pssm-ID: 276957 [Multi-domain]  Cd Length: 430  Bit Score: 39.06  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217268679 117 LHPRSICMIQK------YNHD--------GEAGRLEAFG--QGEsvlkepKYQEELEDRLHFYVEECDYLQGFQILcdlH 180
Cdd:cd02188    67 LEPRVINSIQNspyknlFNPEniylskegGGAGNNWASGysQGE------KVQEEILDIIDREAEGSDSLEGFVLC---H 137

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217268679 181 D-----GfSGVGAKAAELLQDEYSGRGIITWGLLP 210
Cdd:cd02188   138 SiaggtG-SGMGSYLLERLSDRYPKKLIQTYSVFP 171
 
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