NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1958660859|ref|XP_038942748|]
View 

tubulin gamma-2 chain isoform X1 [Rattus norvegicus]

Protein Classification

tubulin gamma chain( domain architecture ID 10115134)

tubulin gamma chain recruits the alpha/beta-tubulin dimers that form the minus ends of microtubules and is thought to be involved in microtubule nucleation and capping

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
37-361 0e+00

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: 687.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLL 116
Cdd:cd02188   109 GEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYPKKLIQTYSVFPNQEESSDVVVQPYNSIL 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLM 196
Cdd:cd02188   189 TLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLISSLIPTPRLHFLM 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 197 TGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRdrqTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIP 276
Cdd:cd02188   269 TSYTPLTSDQVASSVRKTTVLDVMRRLLQPKNRMVSTST---KNGCYISILNIIQGEVDPTQVHKSLQRIRERKLANFIP 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 277 WGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEMDRSREVVQE 356
Cdd:cd02188   346 WGPASIQVALSKKSPYVQTAHRVSGLMLANHTSISSLFEKILSQYDKLRKRNAFLENYRKEDMFQDNLEEFDESREVVQS 425

                  ....*
gi 1958660859 357 LIDEY 361
Cdd:cd02188   426 LIDEY 430
 
Name Accession Description Interval E-value
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
37-361 0e+00

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: 687.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLL 116
Cdd:cd02188   109 GEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYPKKLIQTYSVFPNQEESSDVVVQPYNSIL 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLM 196
Cdd:cd02188   189 TLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLISSLIPTPRLHFLM 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 197 TGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRdrqTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIP 276
Cdd:cd02188   269 TSYTPLTSDQVASSVRKTTVLDVMRRLLQPKNRMVSTST---KNGCYISILNIIQGEVDPTQVHKSLQRIRERKLANFIP 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 277 WGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEMDRSREVVQE 356
Cdd:cd02188   346 WGPASIQVALSKKSPYVQTAHRVSGLMLANHTSISSLFEKILSQYDKLRKRNAFLENYRKEDMFQDNLEEFDESREVVQS 425

                  ....*
gi 1958660859 357 LIDEY 361
Cdd:cd02188   426 LIDEY 430
PLN00222 PLN00222
tubulin gamma chain; Provisional
37-377 0e+00

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 631.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLL 116
Cdd:PLN00222  111 GEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNQMETSDVVVQPYNSLL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLM 196
Cdd:PLN00222  191 TLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLLASLIPTPRCHFLM 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 197 TGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVS--TGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANF 274
Cdd:PLN00222  271 TGYTPLTVERQANVIRKTTVLDVMRRLLQTKNIMVSsyARTKEASQAKYISILNIIQGEVDPTQVHKSLQRIRERKLANF 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 275 IPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDN-FEEMDRSREV 353
Cdd:PLN00222  351 IEWGPASIQVALSRKSPYVQTAHRVSGLMLANHTSIRHLFSKCLSQYDKLRKKQAFLDNYRKFPMFADNdLSEFDESREI 430
                         330       340
                  ....*....|....*....|....
gi 1958660859 354 VQELIDEYHAATRPDYISWGTQEQ 377
Cdd:PLN00222  431 VESLVDEYKACESPDYIKWGMEDP 454
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
190-318 3.87e-65

Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins 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. (The FtsZ GTPases have been split into their won family).


Pssm-ID: 397858 [Multi-domain]  Cd Length: 125  Bit Score: 202.85  E-value: 3.87e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 190 PRLHFLMTGYTPLTTDQSvASVRKTTVLDVMRRLLQPKNVMVSTgRDRqtNHCYIAILNIIQGEVDPTQVHKSLQRIRER 269
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANK-ASHEKTSVLDVTRRLFDPKNQMVSC-DPR--NGKYMACALLYRGDVSPKDVHRAIQRIKEK 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958660859 270 KLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSC 318
Cdd:pfam03953  77 RSAQFVEWCPTGIKVAICSQSPYVVPGSKVSGLMLANTTSIAELFQRLL 125
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
37-173 3.19e-45

Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the bacterial FtsZ family of proteins. These proteins are involved in polymer formation. Tubulin is the major component of microtubules, while 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, this entry is the GTPase domain. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea.


Pssm-ID: 214867 [Multi-domain]  Cd Length: 192  Bit Score: 153.80  E-value: 3.19e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859   37 GEKIHEDIFDIIDREADGSDsleGFVLCHSIAGGTGSGLGSYLLERLNDrYPKKLVqTYSVFPnqdEMSDVVVQPYNSLL 116
Cdd:smart00864  65 GREAAEESLDEIREELEGAD---GVFITAGMGGGTGTGAAPVIAEIAKE-YGILTV-AVVTKP---FSFEGVVRPYNAEL 136
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958660859  117 TLKRLTQNADCVVVLDNTALNRIATDRLhIQNPSFSQINQLVSTIMSASTTTLRYPG 173
Cdd:smart00864 137 GLEELREHVDSLIVIDNDALLDICGRKL-PLRPAFKDANDLLAQAVSGITDLIRFPG 192
 
Name Accession Description Interval E-value
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
37-361 0e+00

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: 687.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLL 116
Cdd:cd02188   109 GEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLERLSDRYPKKLIQTYSVFPNQEESSDVVVQPYNSIL 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLM 196
Cdd:cd02188   189 TLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSLISTVMSASTSTLRFPGYMNNDLVSLISSLIPTPRLHFLM 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 197 TGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVSTGRdrqTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANFIP 276
Cdd:cd02188   269 TSYTPLTSDQVASSVRKTTVLDVMRRLLQPKNRMVSTST---KNGCYISILNIIQGEVDPTQVHKSLQRIRERKLANFIP 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 277 WGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEMDRSREVVQE 356
Cdd:cd02188   346 WGPASIQVALSKKSPYVQTAHRVSGLMLANHTSISSLFEKILSQYDKLRKRNAFLENYRKEDMFQDNLEEFDESREVVQS 425

                  ....*
gi 1958660859 357 LIDEY 361
Cdd:cd02188   426 LIDEY 430
PLN00222 PLN00222
tubulin gamma chain; Provisional
37-377 0e+00

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 631.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMSDVVVQPYNSLL 116
Cdd:PLN00222  111 GEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEALNDRYSKKLVQTYSVFPNQMETSDVVVQPYNSLL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLM 196
Cdd:PLN00222  191 TLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVSTVMSASTTTLRYPGYMNNDLVGLLASLIPTPRCHFLM 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 197 TGYTPLTTDQSVASVRKTTVLDVMRRLLQPKNVMVS--TGRDRQTNHCYIAILNIIQGEVDPTQVHKSLQRIRERKLANF 274
Cdd:PLN00222  271 TGYTPLTVERQANVIRKTTVLDVMRRLLQTKNIMVSsyARTKEASQAKYISILNIIQGEVDPTQVHKSLQRIRERKLANF 350
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 275 IPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDN-FEEMDRSREV 353
Cdd:PLN00222  351 IEWGPASIQVALSRKSPYVQTAHRVSGLMLANHTSIRHLFSKCLSQYDKLRKKQAFLDNYRKFPMFADNdLSEFDESREI 430
                         330       340
                  ....*....|....*....|....
gi 1958660859 354 VQELIDEYHAATRPDYISWGTQEQ 377
Cdd:PLN00222  431 VESLVDEYKACESPDYIKWGMEDP 454
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
37-361 1.17e-117

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: 346.50  E-value: 1.17e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDeMSDVVVQPYNSLL 116
Cdd:cd06059    70 GPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDEYPKVYRFTFSVFPSPD-DDNVITSPYNSVL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRIATD---RLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLH 193
Cdd:cd06059   149 ALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSSLTSSLRFEGSLNVDLNEITTNLVPFPRLH 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 194 FLMTGYTPLTTDQSVaSVRKTTVLDVMRRLLQPKNVMVStgrDRQTNHCYIAILNIIQGEV-DPTQVHKSLQRIRERKla 272
Cdd:cd06059   229 FLLPSLSPLTSANDV-TLEPLTLDQLFSDLFSKDNQLVG---CDPRHGTYLACALLLRGKVfSLSDVRRNIDRIKPKL-- 302
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 273 NFIPWGPASIQVALSRKSPYlpsAHRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEmdrSRE 352
Cdd:cd06059   303 KFISWNPDGFKVGLCSVPPV---GQKYSLLFLSNNTSIASTFERLIERFDKLYKRKAFLHHYTGEGMEEGDFSE---ARE 376

                  ....*....
gi 1958660859 353 VVQELIDEY 361
Cdd:cd06059   377 SLANLIQEY 385
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
36-307 1.99e-110

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: 326.29  E-value: 1.99e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  36 LGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEMsdVVVQPYNSL 115
Cdd:cd00286    69 AGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKDEYPNRLVVTFSILPGPDEG--VIVYPYNAA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 116 LTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFL 195
Cdd:cd00286   147 LTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTEALRFEGSLNVDLRELAENLVPLPRGHFL 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 196 MTGYTPLTTDQSVaSVRKTTVLDVMRRLLQPKNVMVstgRDRQTNHCYIAILNIIQGEVD--PTQVHKSLQRIRERKLAN 273
Cdd:cd00286   227 MLGYAPLDSATSA-TPRSLRVKELTRRAFLPANLLV---GCDPDHGEAIAALLVIRGPPDlsSKEVERAIARVKETLGHL 302
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958660859 274 FiPWGPASIQVALSRKSPYlpsAHRVSGLMMANH 307
Cdd:cd00286   303 F-SWSPAGVKTGISPKPPA---EGEVSVLALLNS 332
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
37-361 5.05e-94

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: 287.54  E-value: 5.05e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNqDEMSDVVVQPYNSLL 116
Cdd:cd02187   108 GAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTLLLSKLREEYPDRIMSTFSVLPS-PKVSDTVVEPYNAVL 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLM 196
Cdd:cd02187   187 SLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLISQVMSGITSSLRFPGQLNSDLRKLATNLVPFPRLHFLT 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 197 TGYTPLTTDQSVASvRKTTVLDVMRRLLQPKNVMVST----GRdrqtnhcYIAILNIIQGEVDPTQVHKSLQRIRERKLA 272
Cdd:cd02187   267 PGFAPLTSRGSQQY-RKLTVPELTQQLFDAKNMMAACdprhGR-------YLTAAAIFRGRISTKEVDEQMSKVQNKNSS 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 273 NFIPWGPASIQVALSRKSPYLPsahRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEmdrSRE 352
Cdd:cd02187   339 YFVEWIPNNVKTSVCDIPPRGL---KMSATFIGNSTAIQELFKRLSEQFTAMFRRKAFLHWYTGEGMDEMEFTE---AES 412

                  ....*....
gi 1958660859 353 VVQELIDEY 361
Cdd:cd02187   413 NLNDLISEY 421
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
36-363 1.23e-81

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: 255.93  E-value: 1.23e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  36 LGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNqDEMSDVVVQPYNSL 115
Cdd:cd02186   109 IGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLERLSVDYGKKSKLEFSIYPS-PQVSTSVVEPYNSV 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 116 LTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFL 195
Cdd:cd02186   188 LTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVVSSLTASLRFDGALNVDLNEFQTNLVPYPRIHFP 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 196 MTGYTPLTTDQSVASVrKTTVLDVMRRLLQPKNVMVSTgrDRQTNHcYIAILNIIQGEVDPTQVHKSLQRIRERKLANFI 275
Cdd:cd02186   268 LVSYAPIISAEKANHE-QLSVQEITNSCFEPANQMVKC--DPRHGK-YMACCLLYRGDVVPKDVNAAIATIKTKRTIQFV 343
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 276 PWGPASIQVALSRKSPYLPSAHRV-----SGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEmdrS 350
Cdd:cd02186   344 DWCPTGFKVGINYQPPTVVPGSDLakvdrSVCMLANSTAIAEAFQRLDHKFDLLYSKRAFVHWYVGEGMEEGEFSE---A 420
                         330
                  ....*....|...
gi 1958660859 351 REVVQELIDEYHA 363
Cdd:cd02186   421 REDLAALEKDYEE 433
PTZ00010 PTZ00010
tubulin beta chain; Provisional
36-361 4.77e-71

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 228.89  E-value: 4.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  36 LGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQdEMSDVVVQPYNSL 115
Cdd:PTZ00010  108 EGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEYPDRIMMTFSVFPSP-KVSDTVVEPYNAT 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 116 LTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFL 195
Cdd:PTZ00010  187 LSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHFF 266
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 196 MTGYTPLTTDQSvASVRKTTVLDVMRRLLQPKNVMVST----GRdrqtnhcYIAILNIIQGEVDPTQVHKSLQRIRERKL 271
Cdd:PTZ00010  267 MMGFAPLTSRGS-QQYRGLSVPELTQQMFDAKNMMCAAdprhGR-------YLTASALFRGRMSTKEVDEQMLNVQNKNS 338
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 272 ANFIPWGPASIQVALSRKSpylPSAHRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEMDRSr 351
Cdd:PTZ00010  339 SYFVEWIPNNIKSSVCDIP---PKGLKMSVTFIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESN- 414
                         330
                  ....*....|
gi 1958660859 352 evVQELIDEY 361
Cdd:PTZ00010  415 --MNDLVSEY 422
Tubulin_C pfam03953
Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. ...
190-318 3.87e-65

Tubulin C-terminal domain; This family includes the tubulin alpha, beta and gamma chains. Members of this family are involved in polymer formation. Tubulins 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. (The FtsZ GTPases have been split into their won family).


Pssm-ID: 397858 [Multi-domain]  Cd Length: 125  Bit Score: 202.85  E-value: 3.87e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 190 PRLHFLMTGYTPLTTDQSvASVRKTTVLDVMRRLLQPKNVMVSTgRDRqtNHCYIAILNIIQGEVDPTQVHKSLQRIRER 269
Cdd:pfam03953   1 PRLHFLLTSYAPLTSANK-ASHEKTSVLDVTRRLFDPKNQMVSC-DPR--NGKYMACALLYRGDVSPKDVHRAIQRIKEK 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958660859 270 KLANFIPWGPASIQVALSRKSPYLPSAHRVSGLMMANHTSISSLFESSC 318
Cdd:pfam03953  77 RSAQFVEWCPTGIKVAICSQSPYVVPGSKVSGLMLANTTSIAELFQRLL 125
PLN00220 PLN00220
tubulin beta chain; Provisional
37-361 1.83e-64

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 211.99  E-value: 1.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQdEMSDVVVQPYNSLL 116
Cdd:PLN00220  109 GAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSP-KVSDTVVEPYNATL 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFLM 196
Cdd:PLN00220  188 SVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFM 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 197 TGYTPLTTDQSvASVRKTTVLDVMRRLLQPKNVMVST----GRdrqtnhcYIAILNIIQGEVDPTQVHKSLQRIRERKLA 272
Cdd:PLN00220  268 VGFAPLTSRGS-QQYRALTVPELTQQMWDAKNMMCAAdprhGR-------YLTASAMFRGKMSTKEVDEQMINVQNKNSS 339
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 273 NFIPWGPASIQVALSRKSPylpsahrvSGLMMA-----NHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEM 347
Cdd:PLN00220  340 YFVEWIPNNVKSSVCDIPP--------KGLKMAstfigNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEA 411
                         330
                  ....*....|....
gi 1958660859 348 DRSrevVQELIDEY 361
Cdd:PLN00220  412 ESN---MNDLVSEY 422
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
37-363 7.34e-62

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: 205.17  E-value: 7.34e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEmsDVVVQPYNSLL 116
Cdd:cd02190   115 GPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGSGLGSYILELLEDEFPDVYRFVTSVFPSGDD--DVITSPYNSVL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRI----------------ATDRLHIQNP------SFSQINQLVSTIMSASTTTLRYPGY 174
Cdd:cd02190   193 ALRELTEHADCVLPVENQALMDIvnkiksskdkgktgvlAAINSSGGGQkkgkkkPFDDMNNIVANLLLNLTSSMRFEGS 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 175 MNNDLIGLIASLIPTPRLHFLMTGYTPL--TTDQSVASVRkttvLDVM-RRLLQPKNVMVSTGRDRqtnHCYIAILNIIQ 251
Cdd:cd02190   273 LNVDLNEITTNLVPFPRLHFLLSSLSPLyaLADVRLPPRR----LDQMfSDAFSRDHQLLKADPKH---GLYLACALLVR 345
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 252 GEVDPTQVHKSLQRIReRKLaNFIPWGPASIQVALSRKSpylPSAHRVSGLMMANHTSISSLFESSCQQYDKLWKRGAFL 331
Cdd:cd02190   346 GNVSISDLRRNIDRLK-RQL-KFVSWNQDGWKIGLCSVP---PVGQPYSLLCLANNTCIKPTFTEMHERFDKLYKRKAHL 420
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1958660859 332 ---EQFRKEDIFKDnfeemdrSREVVQELIDEYHA 363
Cdd:cd02190   421 hhyTQYMEQDDFDE-------ALESLLDLIEEYKD 448
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
36-361 2.23e-60

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 201.09  E-value: 2.23e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  36 LGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNqDEMSDVVVQPYNSL 115
Cdd:PTZ00335  110 IGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPS-PQVSTAVVEPYNSV 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 116 LTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFL 195
Cdd:PTZ00335  189 LSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISSLTASLRFDGALNVDLTEFQTNLVPYPRIHFM 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 196 MTGYTPLTTDQSvASVRKTTVLDVMRRLLQPKNVMV----STGRdrqtnhcYIAILNIIQGEVDPTQVHKSLQRIRERKL 271
Cdd:PTZ00335  269 LSSYAPIISAEK-AYHEQLSVAEITNSAFEPANMMAkcdpRHGK-------YMACCLMYRGDVVPKDVNAAIATIKTKRT 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 272 ANFIPWGPASIQVALSRKSP-YLPSAH--RV--SGLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEE 346
Cdd:PTZ00335  341 IQFVDWCPTGFKCGINYQPPtVVPGGDlaKVqrAVCMISNSTAIAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSE 420
                         330
                  ....*....|....*
gi 1958660859 347 mdrSREVVQELIDEY 361
Cdd:PTZ00335  421 ---AREDLAALEKDY 432
PTZ00387 PTZ00387
epsilon tubulin; Provisional
37-361 3.20e-59

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 198.79  E-value: 3.20e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  37 GEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQDEmsDVVVQPYNSLL 116
Cdd:PTZ00387  110 GDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILGMLEDEFPHVFRFCPVVFPSAVD--DVITSPYNSFF 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 117 TLKRLTQNADCVVVLDNTALNRIA-------TDRLHIQNPS--------------------FSQINQLVSTIMSASTTTL 169
Cdd:PTZ00387  188 ALRELIEHADCVLPLDNDALANIAdsalsrkKKKLAKGNIKrgpqphkysvakptetkklpYDKMNNIVAQLLSNLTSSM 267
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 170 RYPGYMNNDLIGLIASLIPTPRLHFLMTGYTPLTTDQSVASVRKTtvLDVM-RRLLQPKNVMVSTGRDRqtnHCYIAILN 248
Cdd:PTZ00387  268 RFEGSLNVDINEITTNLVPYPRLHFLTSSIAPLVSLKDVAVGPRR--LDQMfKDCLDPDHQMVAATPEA---GKYLATAL 342
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 249 IIQGEVDPTQVHKSLQRIRERKlaNFIPWGPASIQVALSRKSPYlpsAHRVSGLMMANHTSISSLFESSCQQYDKLWKRG 328
Cdd:PTZ00387  343 IVRGPQNVSDVTRNILRLKEQL--NMIYWNEDGFKTGLCNVSPL---GQPYSLLCLANNCCIRNKFESMLERFNKLYKRK 417
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1958660859 329 AFL---EQFRKEDIFkdnfeemDRSREVVQELIDEY 361
Cdd:PTZ00387  418 SHVhhyTEYLEQAYF-------DETLETIQNLIDDY 446
PLN00221 PLN00221
tubulin alpha chain; Provisional
36-361 6.12e-51

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 176.54  E-value: 6.12e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  36 LGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNQdEMSDVVVQPYNSL 115
Cdd:PLN00221  110 IGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSP-QVSTAVVEPYNSV 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 116 LTLKRLTQNADCVVVLDNTALNRIATDRLHIQNPSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGLIASLIPTPRLHFL 195
Cdd:PLN00221  189 LSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQVISSLTASLRFDGALNVDITEFQTNLVPYPRIHFM 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 196 MTGYTPLTTDQSvASVRKTTVLDVMRRLLQPKNVMVSTGRDRQTnhcYIAILNIIQGEVDPTQVHKSLQRIRERKLANFI 275
Cdd:PLN00221  269 LSSYAPVISAEK-AYHEQLSVAEITNSAFEPASMMAKCDPRHGK---YMACCLMYRGDVVPKDVNAAVATIKTKRTIQFV 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 276 PWGPASIQVALSRKSPY------LPSAHRVSgLMMANHTSISSLFESSCQQYDKLWKRGAFLEQFRKEDIFKDNFEEmdr 349
Cdd:PLN00221  345 DWCPTGFKCGINYQPPTvvpggdLAKVQRAV-CMISNSTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEFSE--- 420
                         330
                  ....*....|..
gi 1958660859 350 SREVVQELIDEY 361
Cdd:PLN00221  421 AREDLAALEKDY 432
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
36-363 1.16e-47

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: 167.44  E-value: 1.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  36 LGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNqdEMSDVVVQPYNSL 115
Cdd:cd02189   102 HGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDEYPKAYLLNTVVWPY--SSGEVPVQNYNTL 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 116 LTLKRLTQNADCVVVLDNTALNRIATDRLHIQNP-SFSQINQLVST-----IMSASTTTLRYPGYMNNdLIGLIASLIPT 189
Cdd:cd02189   180 LTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARqlagvLLPSSSPTSPSPLRRCP-LGDLLEHLCPH 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 190 PRLHFLMTGYTPLTTDQSVASVRkTTVLDVMRRLLQ----------PKNVMVSTGRDRQTNHCYIAILNIIQGEvDPTQV 259
Cdd:cd02189   259 PAYKLLTLRSLPQMPEPSRAFST-YTWPSLLKRLRQmlitgakleeGIDWQLLDTSGSHNPNKSLAALLVLRGK-DAMKV 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 260 HKSLQRIReRKLANFIPWGPASIQVALSRKSP--YLPSAhrvsgLMMANHTSI----SSLFESSCQQYDKlwkrGAFLEQ 333
Cdd:cd02189   337 HSADLSAF-KDPVLYSPWVPNPFNVSVSPRPFngYEKSV-----TLLSNSQNIvgplDSLLEKAWQMFKA----GAYLHQ 406
                         330       340       350
                  ....*....|....*....|....*....|
gi 1958660859 334 FRKEDIFKDNFEEmdrSREVVQELIDEYHA 363
Cdd:cd02189   407 YEKYGVEEEDFLD---AFATLEQIIAAYKS 433
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
37-173 3.19e-45

Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the bacterial FtsZ family of proteins. These proteins are involved in polymer formation. Tubulin is the major component of microtubules, while 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, this entry is the GTPase domain. FtsZ can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea.


Pssm-ID: 214867 [Multi-domain]  Cd Length: 192  Bit Score: 153.80  E-value: 3.19e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859   37 GEKIHEDIFDIIDREADGSDsleGFVLCHSIAGGTGSGLGSYLLERLNDrYPKKLVqTYSVFPnqdEMSDVVVQPYNSLL 116
Cdd:smart00864  65 GREAAEESLDEIREELEGAD---GVFITAGMGGGTGTGAAPVIAEIAKE-YGILTV-AVVTKP---FSFEGVVRPYNAEL 136
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958660859  117 TLKRLTQNADCVVVLDNTALNRIATDRLhIQNPSFSQINQLVSTIMSASTTTLRYPG 173
Cdd:smart00864 137 GLEELREHVDSLIVIDNDALLDICGRKL-PLRPAFKDANDLLAQAVSGITDLIRFPG 192
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
36-140 1.60e-41

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: 144.28  E-value: 1.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  36 LGEKIHEDIFDIIDREADGSDSLEGFVLCHSIAGGTGSGLGSYLLERLNDRYPKKLVQTYSVFPNqdEMSDVVVQPYNSL 115
Cdd:pfam00091  87 IGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKELYPGALTVAVVTFPF--GFSEGVVRPYNAI 164
                          90       100
                  ....*....|....*....|....*
gi 1958660859 116 LTLKRLTQNADCVVVLDNTALNRIA 140
Cdd:pfam00091 165 LGLKELIEHSDSVIVIDNDALYDIC 189
Tubulin_C smart00865
Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and ...
175-315 3.23e-18

Tubulin/FtsZ family, C-terminal domain; This domain is found in the tubulin alpha, beta and gamma chains, as well as the bacterial FtsZ family of proteins. These proteins are GTPases and are involved in polymer formation. Tubulin is the major component of microtubules, while 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 can polymerise into tubes, sheets, and rings in vitro and is ubiquitous in bacteria and archaea. This is the C-terminal domain.


Pssm-ID: 214868 [Multi-domain]  Cd Length: 120  Bit Score: 79.52  E-value: 3.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  175 MNNDLIGLIASLIPTPrlhFLMTGYTPLTTDqsvasVRKTTVLDVMR--RLLQPKNVMVSTGrdrqtnhcyiAILNIIQG 252
Cdd:smart00865   1 INVDFADVKTVMVPMG---FAMMGIGPASGE-----NRALEAAELAIssPLLEDSNIMGAKG----------VLVNITGG 62
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958660859  253 -EVDPTQVHKSLQRIRERKL-ANFIPWGPASIQVALsrkspylpsahrVSGLMMAN-HTSISSLFE 315
Cdd:smart00865  63 pDLTLKEVNEAMERIREKADpDAFIIWGPVIDEELG------------GDEIRVTViATGIGSLFK 116
CetZ_tubulin-like cd02202
Cell-structure-related euryarchaeota tubulin/FtsZ homologs; CetZ proteins comprise a distinct ...
38-142 2.24e-08

Cell-structure-related euryarchaeota tubulin/FtsZ homologs; CetZ proteins comprise a distinct tubulin/FtsZ family. The crystal structures of CetZ contain the FtsZ/tubulin superfamily fold and its family members have mosaic of tubulin-like and FtsZ-like amino acid residues. However, 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: 276962 [Multi-domain]  Cd Length: 357  Bit Score: 55.33  E-value: 2.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  38 EKIHEDIFDIIDREADGsdslegFVLCHSIAGGTGSGLGSYLLERLNDRYPkKLVQTYSVFPNQDEmSDVVVqpYNSLLT 117
Cdd:cd02202    84 DELLRALDTAPFSEADA------FLVVAGLGGGTGSGAAPVLAEELKERYD-KPVYALGVLPAAEE-GGRYA--LNAARS 153
                          90       100
                  ....*....|....*....|....*
gi 1958660859 118 LKRLTQNADCVVVLDNTALNRIATD 142
Cdd:cd02202   154 LRSLVELADAVILFDNDAWRRSGES 178
FtsZ_CetZ-like cd02191
Subfamily of FitZ and Cell-structure-related euryarchaeota tubulin/FtsZ homolog-like; FtsZ is ...
23-261 3.48e-06

Subfamily of FitZ and Cell-structure-related euryarchaeota tubulin/FtsZ homolog-like; FtsZ is a GTPase that is similar to the eukaryotic tubulins and is essential for cell division in prokaryotes. CetZ-like proteins are related to tubulin and FtsZ and co-exists with FtsZ in many archaea. However, a recent study found that Cetz proteins (formerly annotated FtsZ type 2) are not required for cell division. 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: 276960 [Multi-domain]  Cd Length: 308  Bit Score: 48.33  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  23 GPGDSPRCQSQTFLGEKihEDIFDIIDREADgSDSLegFVLChSIAGGTGSGLGSYLLERLNDRYpKKLVQTYSVFPNQD 102
Cdd:cd02191    64 GVGGNPELGAQAAEEDQ--EEIMEALEGRVE-ADMI--FVTT-GLGGGTGSGGAPVLAEALKKVY-DVLTVAVVTLPFAD 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 103 EMSdvvVQPYNSLLTLKRLTQNADCVVVLDNTALNRIATDRLHiqnpSFSQINQLVSTIMSASTTTLRYPGYMNNDLIGL 182
Cdd:cd02191   137 EGA---LYMQNAGEGLRTLAEEADALILVDNEKLRSIGGSLSE----AYDAINEVLARRVGGLLEAIEATGLSVVDFADV 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859 183 IASLiptPRLHFLMTGYTplTTDQSVASVRKTTVLDVMRRLLQPKN-------VMVSTGRDRQTNHCYIAILNIIQGEVD 255
Cdd:cd02191   210 KTVM---NSGGMAMLGYG--SADASINRAREATRRALRTPLLLPDAsgadgalVVIAGEPDTLPLKEVERVRRWVEDETG 284

                  ....*.
gi 1958660859 256 PTQVHK 261
Cdd:cd02191   285 SATVRG 290
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
56-171 6.15e-06

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: 48.08  E-value: 6.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958660859  56 DSLEGF-VLCHSIAGGtgSGLGSYLLERLNDRYPKKLVQTY---SVFPNQDEMSDVVVQPYNSLLTLKRLTQNADCVVVL 131
Cdd:cd06060   205 DSLQGFqILVDTDDGF--GGVAAKLLENLRDEYGKKSILTPglsPASPPDPDSQRRIKRLLNDALSLSSLSEHSSLFVPL 282
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958660859 132 DNTALNRIATDRLhiqnPSFSQINQL----VSTIMSAS--TTTLRY 171
Cdd:cd06060   283 SLPSLLWRKPGWP----RTFPHLDYSspyhTSAVLAAAldTATLPY 324
FtsZ_type1 cd02201
Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the ...
118-179 5.19e-03

Filamenting temperature sensitive mutant Z, type 1; FtsZ is a GTPase that is similar to the eukaryotic tubulins and is essential for cell division in prokaryotes. FtsZ is capable of polymerizing in a GTP-driven process into structures similar to those formed by tubulin. 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.


Pssm-ID: 276961 [Multi-domain]  Cd Length: 303  Bit Score: 38.53  E-value: 5.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958660859 118 LKRLTQNADCVVVLDNTALNRIATDRLHIQNpSFSQINQLVSTIMSASTTTLRYPGYMNNDL 179
Cdd:cd02201   140 LEELKKYVDTLIVIPNDKLLEIVGKNLPLLE-AFKKADEVLAQAVKGITDLITKPGLINLDF 200
 
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