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Conserved domains on  [gi|19115570|ref|NP_594658|]
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GTPase dml1 [Schizosaccharomyces pombe]

Protein Classification

FtsZ/tubulin family protein( domain architecture ID 3)

FtsZ/tubulin family protein may be involved in polymer formation, similar to the cell-division GTPase FtsZ or the tubulin-like filament-forming GTPase TubZ

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Tubulin_FtsZ_Cetz-like super family cl10017
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
2-332 4.93e-55

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.


The actual alignment was detected with superfamily member cd06060:

Pssm-ID: 471962 [Multi-domain]  Cd Length: 539  Bit Score: 191.76  E-value: 4.93e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570   2 HEILTVTFGRKSNFCWTHFWNTQESYFVYDPNDHAKV---NVNTNFRVlkKRDPEAIVT-VPRECIYDTPIEFGNTRK-N 76
Cdd:cd06060   1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPdhdVHDVLFRE--GETLQGEETyTPRLLLVDLKGSLGSLRKeG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570  77 WLEELNESSGGkGTAWDGKLTQIMQTPVDVHPYQEALWSRDEIHEGNAIESEYELPSIRPK---SVKYWSDFNRLfldte 153
Cdd:cd06060  79 ALYEEPDDDSS-ESQWWGDVETHVQEPIEKNEFQQDLEEEETYQVELESQSTAEDGDKVYLleeSVRVWSDYLRV----- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570 154 YLFPVNCSELN-------SSDF-SFQLGVERFHDFDkQFNVWDEGLRPLVEECDSVQGFQAAIDIDTPWGGFASEYMKVV 225
Cdd:cd06060 153 YYHPRSINVLNeyqhdseFNPFdNFSQGEELFSDLE-ELEEFEDRLRFFVEECDSLQGFQILVDTDDGFGGVAAKLLENL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570 226 QDELGecRVPTWVYGIREPIQSDSSATIDNHFgKLNEALSLSQLNGSCSQYFPLCTISQG---------------DDLWA 290
Cdd:cd06060 232 RDEYG--KKSILTPGLSPASPPDPDSQRRIKR-LLNDALSLSSLSEHSSLFVPLSLPSLLwrkpgwprtfphldySSPYH 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 19115570 291 SSAKINLAIESFTLPTRVYGSSCyRMKDIESKLQSEGRGFIH 332
Cdd:cd06060 309 TSAVLAAALDTATLPYRLKSSSV-SMSDLCSSLTFSGRKVAA 349
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
2-332 4.93e-55

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: 191.76  E-value: 4.93e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570   2 HEILTVTFGRKSNFCWTHFWNTQESYFVYDPNDHAKV---NVNTNFRVlkKRDPEAIVT-VPRECIYDTPIEFGNTRK-N 76
Cdd:cd06060   1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPdhdVHDVLFRE--GETLQGEETyTPRLLLVDLKGSLGSLRKeG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570  77 WLEELNESSGGkGTAWDGKLTQIMQTPVDVHPYQEALWSRDEIHEGNAIESEYELPSIRPK---SVKYWSDFNRLfldte 153
Cdd:cd06060  79 ALYEEPDDDSS-ESQWWGDVETHVQEPIEKNEFQQDLEEEETYQVELESQSTAEDGDKVYLleeSVRVWSDYLRV----- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570 154 YLFPVNCSELN-------SSDF-SFQLGVERFHDFDkQFNVWDEGLRPLVEECDSVQGFQAAIDIDTPWGGFASEYMKVV 225
Cdd:cd06060 153 YYHPRSINVLNeyqhdseFNPFdNFSQGEELFSDLE-ELEEFEDRLRFFVEECDSLQGFQILVDTDDGFGGVAAKLLENL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570 226 QDELGecRVPTWVYGIREPIQSDSSATIDNHFgKLNEALSLSQLNGSCSQYFPLCTISQG---------------DDLWA 290
Cdd:cd06060 232 RDEYG--KKSILTPGLSPASPPDPDSQRRIKR-LLNDALSLSSLSEHSSLFVPLSLPSLLwrkpgwprtfphldySSPYH 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 19115570 291 SSAKINLAIESFTLPTRVYGSSCyRMKDIESKLQSEGRGFIH 332
Cdd:cd06060 309 TSAVLAAALDTATLPYRLKSSSV-SMSDLCSSLTFSGRKVAA 349
Tubulin_3 pfam14881
Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ...
132-307 1.03e-50

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: 170.25  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570   132 PSIRPKSVKYWSDFNRLFLDTEYLFPVNCSELNSSDFSFQ---LGVERFHDFDKQFNVWDEGLRPLVEECDSVQGFQAAI 208
Cdd:pfam14881   2 PQLTTSTVRYWSDFNRVFYHPRSIVQLNEYELNSQLMPFEdwsVGEELFRELDKEHDLLDRDLRPFAEECDQLQGLQVFT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570   209 DIDTPWGGFASEYMKVVQDELGECRVpTWVYGIREPIQSDSSATIDNHFGKLNEALSLSQLNGSCSQYFPLCTISQGDDL 288
Cdd:pfam14881  82 GSDDAWGGFAARYLERLRDEYGKKSI-IWVWALQDPLKRIRRTKRERRLRLANKARSLQSLSPQASLYVPIATLSDGQSE 160
                         170
                  ....*....|....*....
gi 19115570   289 WASSAKINLAIESFTLPTR 307
Cdd:pfam14881 161 WHTSALLSSAIESATLPSR 179
 
Name Accession Description Interval E-value
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
2-332 4.93e-55

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: 191.76  E-value: 4.93e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570   2 HEILTVTFGRKSNFCWTHFWNTQESYFVYDPNDHAKV---NVNTNFRVlkKRDPEAIVT-VPRECIYDTPIEFGNTRK-N 76
Cdd:cd06060   1 REIVTLQLGHYANFVGTHFWNIQESYFTYDEDEEAPPdhdVHDVLFRE--GETLQGEETyTPRLLLVDLKGSLGSLRKeG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570  77 WLEELNESSGGkGTAWDGKLTQIMQTPVDVHPYQEALWSRDEIHEGNAIESEYELPSIRPK---SVKYWSDFNRLfldte 153
Cdd:cd06060  79 ALYEEPDDDSS-ESQWWGDVETHVQEPIEKNEFQQDLEEEETYQVELESQSTAEDGDKVYLleeSVRVWSDYLRV----- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570 154 YLFPVNCSELN-------SSDF-SFQLGVERFHDFDkQFNVWDEGLRPLVEECDSVQGFQAAIDIDTPWGGFASEYMKVV 225
Cdd:cd06060 153 YYHPRSINVLNeyqhdseFNPFdNFSQGEELFSDLE-ELEEFEDRLRFFVEECDSLQGFQILVDTDDGFGGVAAKLLENL 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570 226 QDELGecRVPTWVYGIREPIQSDSSATIDNHFgKLNEALSLSQLNGSCSQYFPLCTISQG---------------DDLWA 290
Cdd:cd06060 232 RDEYG--KKSILTPGLSPASPPDPDSQRRIKR-LLNDALSLSSLSEHSSLFVPLSLPSLLwrkpgwprtfphldySSPYH 308
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 19115570 291 SSAKINLAIESFTLPTRVYGSSCyRMKDIESKLQSEGRGFIH 332
Cdd:cd06060 309 TSAVLAAALDTATLPYRLKSSSV-SMSDLCSSLTFSGRKVAA 349
Tubulin_3 pfam14881
Tubulin domain; This family includes the tubulin alpha, beta and gamma chains, as well as the ...
132-307 1.03e-50

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: 170.25  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570   132 PSIRPKSVKYWSDFNRLFLDTEYLFPVNCSELNSSDFSFQ---LGVERFHDFDKQFNVWDEGLRPLVEECDSVQGFQAAI 208
Cdd:pfam14881   2 PQLTTSTVRYWSDFNRVFYHPRSIVQLNEYELNSQLMPFEdwsVGEELFRELDKEHDLLDRDLRPFAEECDQLQGLQVFT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570   209 DIDTPWGGFASEYMKVVQDELGECRVpTWVYGIREPIQSDSSATIDNHFGKLNEALSLSQLNGSCSQYFPLCTISQGDDL 288
Cdd:pfam14881  82 GSDDAWGGFAARYLERLRDEYGKKSI-IWVWALQDPLKRIRRTKRERRLRLANKARSLQSLSPQASLYVPIATLSDGQSE 160
                         170
                  ....*....|....*....
gi 19115570   289 WASSAKINLAIESFTLPTR 307
Cdd:pfam14881 161 WHTSALLSSAIESATLPSR 179
Misat_Tub_SegII pfam10644
Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved ...
2-115 2.12e-43

Misato Segment II tubulin-like domain; The misato protein contains three distinct, conserved domains, segments I, II and III. Segments I and III are common to Tubulins pfam00091, but segment II aligns with myosin heavy chain sequences from D. melanogaster (PIR C35815), rabbit (SP P04460), and human (PIR S12458). Segment II of misato is a major contributor to its greater length compared with the various tubulins. The most significant sequence similarities to this 54-amino acid region are from a motif found in the heavy chains of myosins from different organizms. A comparison of segment II with the vertebrate myosin heavy chains reveals that it is homologous to a myosin peptide in the hinge region linking the S2 and LMM domains. Segment II also contains heptad repeats which are characteriztic of the myosin tail alpha-helical coiled-coils. This myosin-like homology may be due only to the fact that both myosin and Misato carry coiled-coils, which appear similar but are not necessarily homologous (Wood V, personal communication).


Pssm-ID: 431412 [Multi-domain]  Cd Length: 115  Bit Score: 148.55  E-value: 2.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19115570     2 HEILTVTFGRKSNFCWTHFWNTQESYFVYDPNDH-AKVNVNTNFRVLKKRDpEAIVTVPRECIYDTPIEFGNTRK-NWLE 79
Cdd:pfam10644   1 REIITLQFGNYSNYVGTHFWNTQESYFTYDPNEEpSEVDHDVLFREGETLD-GQVTYTPRLLIYDLKGSFGSLRKeGALY 79
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 19115570    80 ELNESSGGKGTAWDGKLTQIMQTPVDVHPYQEALWS 115
Cdd:pfam10644  80 ELNESAGSNAATWDGKVVVQRQPPIEKSEYQQSLDK 115
 
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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