NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|50592998|ref|NP_057345|]
View 

tubulin delta chain isoform 1 [Homo sapiens]

Protein Classification

tubulin family protein( domain architecture ID 10115139)

tubulin family protein similar to tubulin delta chain that acts as a positive regulator of hedgehog signaling and regulates ciliary function

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
2-452 0e+00

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: 630.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   2 SIVTVQLGQCGNQIGFEVFDALLSDSHSSQglcsmreNEAYQASCKERFFSEEENGVPIARAVLVDMEPKVINQMLSKAA 81
Cdd:cd02189   1 SIVTVQVGQCGNQLGDELFDTLADEADSSA-------SEGDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRAR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  82 qSGQWKYGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNLEDQ 161
Cdd:cd02189  74 -SGAWSYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 162 YSNSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQI-SFSDINQVLAHQLGSVFQ 240
Cdd:cd02189 153 YPKAYLLNTVVWPYSSGEVPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVLL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 241 PTYSAESSFHYRRNPLGDLMEHLVPHPEFKMLSVRNIPHMSENSLAYTTFTWAGLLKHLRQMLISNAKMEEGIDRHvwpp 320
Cdd:cd02189 233 PSSSPTSPSPLRRCPLGDLLEHLCPHPAYKLLTLRSLPQMPEPSRAFSTYTWPSLLKRLRQMLITGAKLEEGIDWQ---- 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 321 lsglpplsKMSLNKDLHFNTSIANLVILRGKD---VQSADVEGFKDPALYTSWLKpvNAFNVWKTQRAFSKYEKSAVLVS 397
Cdd:cd02189 309 --------LLDTSGSHNPNKSLAALLVLRGKDamkVHSADLSAFKDPVLYSPWVP--NPFNVSVSPRPFNGYEKSVTLLS 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 50592998 398 NSQFLVKPLDMIVGKAWNMFASKAYIHQYTKFGIEEEDFLDSFTSLEQVVASYCN 452
Cdd:cd02189 379 NSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATLEQIIAAYKS 433
 
Name Accession Description Interval E-value
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
2-452 0e+00

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: 630.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   2 SIVTVQLGQCGNQIGFEVFDALLSDSHSSQglcsmreNEAYQASCKERFFSEEENGVPIARAVLVDMEPKVINQMLSKAA 81
Cdd:cd02189   1 SIVTVQVGQCGNQLGDELFDTLADEADSSA-------SEGDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRAR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  82 qSGQWKYGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNLEDQ 161
Cdd:cd02189  74 -SGAWSYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 162 YSNSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQI-SFSDINQVLAHQLGSVFQ 240
Cdd:cd02189 153 YPKAYLLNTVVWPYSSGEVPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVLL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 241 PTYSAESSFHYRRNPLGDLMEHLVPHPEFKMLSVRNIPHMSENSLAYTTFTWAGLLKHLRQMLISNAKMEEGIDRHvwpp 320
Cdd:cd02189 233 PSSSPTSPSPLRRCPLGDLLEHLCPHPAYKLLTLRSLPQMPEPSRAFSTYTWPSLLKRLRQMLITGAKLEEGIDWQ---- 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 321 lsglpplsKMSLNKDLHFNTSIANLVILRGKD---VQSADVEGFKDPALYTSWLKpvNAFNVWKTQRAFSKYEKSAVLVS 397
Cdd:cd02189 309 --------LLDTSGSHNPNKSLAALLVLRGKDamkVHSADLSAFKDPVLYSPWVP--NPFNVSVSPRPFNGYEKSVTLLS 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 50592998 398 NSQFLVKPLDMIVGKAWNMFASKAYIHQYTKFGIEEEDFLDSFTSLEQVVASYCN 452
Cdd:cd02189 379 NSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATLEQIIAAYKS 433
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
2-213 2.55e-68

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: 215.93  E-value: 2.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998     2 SIVTVQLGQCGNQIGFEVFDALLSDshssqglcsmreneaYQASCKERFFSEEENGVPIARAVLVDMEPKVINQMLSKaa 81
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLE---------------HGIDSLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG-- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    82 qsgqwkYGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNLEDQ 161
Cdd:pfam00091  64 ------FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKEL 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 50592998   162 YSNSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKIC 213
Cdd:pfam00091 138 YPGALTVAVVTFPFGFSEGVVRPYNAILGLKELIEHSDSVIVIDNDALYDIC 189
PTZ00387 PTZ00387
epsilon tubulin; Provisional
3-242 1.58e-49

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 175.30  E-value: 1.58e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    3 IVTVQLGQCGNQIGFEVFDALLSDsHSSQGlcsmrENEAYQASCKERFFSEEENGVPI------ARAVLVDMEPKVINQM 76
Cdd:PTZ00387   4 IVTVQVGQCGNQLGHRFWDVALKE-HKKIN-----ANPQYDDARDSFFENVSENVNRPgkenlkARAVLVDMEEGVLNQI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   77 LSKAAQSgqwKYGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQ 156
Cdd:PTZ00387  78 LKSPLGD---LFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  157 NLEDQYSNSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKIC--AKLMNIKQISFSDINQVLAHQ 234
Cdd:PTZ00387 155 MLEDEFPHVFRFCPVVFPSAVDDVITSPYNSFFALRELIEHADCVLPLDNDALANIAdsALSRKKKKLAKGNIKRGPQPH 234

                 ....*...
gi 50592998  235 LGSVFQPT 242
Cdd:PTZ00387 235 KYSVAKPT 242
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
47-238 3.04e-40

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: 142.63  E-value: 3.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998     47 KERFFSEEeNGVPiaRAVLVDMEPKVINQMLSKaaqsgqwKYGQH----ACFCQKQGSGNNWAYGYSV-----HGPRHEE 117
Cdd:smart00864   1 KIKVFGVG-GGGP--NAVNVDLEPGVIDGVRAN-------TDAQAlnpeSLASGKIQAGNNWTRGLGAgadpeVGREAAE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    118 SIMNIIRKEVEKCDsfsGFFIIMSMAGGTGSGLGAFVTQNLEDQysNSLKMNQIIWPyGTGEVIVQNYNSILTLSHLYRS 197
Cdd:smart00864  71 ESLDEIREELEGAD---GVFITAGMGGGTGTGAAPVIAEIAKEY--GILTVAVVTKP-FSFEGVVRPYNAELGLEELREH 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 50592998    198 SDALLLHENDAIHKICAKLmNIKQISFSDINQVLAHQLGSV 238
Cdd:smart00864 145 VDSLIVIDNDALLDICGRK-LPLRPAFKDANDLLAQAVSGI 184
 
Name Accession Description Interval E-value
delta_zeta_tubulin-like cd02189
The delta- and zeta-tubulin families; The tubulin superfamily includes five distinct families, ...
2-452 0e+00

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: 630.07  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   2 SIVTVQLGQCGNQIGFEVFDALLSDSHSSQglcsmreNEAYQASCKERFFSEEENGVPIARAVLVDMEPKVINQMLSKAA 81
Cdd:cd02189   1 SIVTVQVGQCGNQLGDELFDTLADEADSSA-------SEGDQNSSATRFFSPFSDGKLKARCVLVDMEPKVVQQVLSRAR 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  82 qSGQWKYGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNLEDQ 161
Cdd:cd02189  74 -SGAWSYDPKNVVCGQSGSGNNWALGYYVHGPSLLEDILEALRREAERCDRLSGFLVLHSLAGGTGSGLGSRVTELLRDE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 162 YSNSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQI-SFSDINQVLAHQLGSVFQ 240
Cdd:cd02189 153 YPKAYLLNTVVWPYSSGEVPVQNYNTLLTLSHLQESSDGILLFENDDLHKICSKLLGLKNPvSFSDINRVIARQLAGVLL 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 241 PTYSAESSFHYRRNPLGDLMEHLVPHPEFKMLSVRNIPHMSENSLAYTTFTWAGLLKHLRQMLISNAKMEEGIDRHvwpp 320
Cdd:cd02189 233 PSSSPTSPSPLRRCPLGDLLEHLCPHPAYKLLTLRSLPQMPEPSRAFSTYTWPSLLKRLRQMLITGAKLEEGIDWQ---- 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 321 lsglpplsKMSLNKDLHFNTSIANLVILRGKD---VQSADVEGFKDPALYTSWLKpvNAFNVWKTQRAFSKYEKSAVLVS 397
Cdd:cd02189 309 --------LLDTSGSHNPNKSLAALLVLRGKDamkVHSADLSAFKDPVLYSPWVP--NPFNVSVSPRPFNGYEKSVTLLS 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*
gi 50592998 398 NSQFLVKPLDMIVGKAWNMFASKAYIHQYTKFGIEEEDFLDSFTSLEQVVASYCN 452
Cdd:cd02189 379 NSQNIVGPLDSLLEKAWQMFKAGAYLHQYEKYGVEEEDFLDAFATLEQIIAAYKS 433
Tubulin_FtsZ_Cetz-like cd00286
Tubulin protein family of FtsZ and CetZ-like; This family includes tubulin alpha-, beta-, ...
2-399 4.86e-131

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: 381.37  E-value: 4.86e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   2 SIVTVQLGQCGNQIGFEVFDAllsdshssqglcsmreneayqasckerffseeengvpiarAVLVDMEPKVINQMLSKAA 81
Cdd:cd00286   1 EIVTIQVGQCGNQIGAAFWEQ----------------------------------------AVLVDLEPAVLDELLSGPL 40
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  82 qsGQWKYGQHACFCQK-QGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNLED 160
Cdd:cd00286  41 --RQLFHPENIILIQKyHGAGNNWAKGHSVAGEEYQEEILDAIRKEVEECDELQGFFITHSLGGGTGSGLGPLLAERLKD 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 161 QYSNSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQISFSDINQVLAHQLGSVFQ 240
Cdd:cd00286 119 EYPNRLVVTFSILPGPDEGVIVYPYNAALTLKTLTEHADCLLLVDNEALYDICPRPLHIDAPAYDHINELVAQRLGSLTE 198
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 241 PTYSAESSFHYrrnpLGDLMEHLVPHPEFKMLSVRNIPHMSENSLayttFTWAGLLKHLRQMLISNAKMEEGidrhvwpp 320
Cdd:cd00286 199 ALRFEGSLNVD----LRELAENLVPLPRGHFLMLGYAPLDSATSA----TPRSLRVKELTRRAFLPANLLVG-------- 262
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 321 lsglpplskmslnKDLHFNTSIANLVILRGK-DVQSADVEGFKDPALYTSWLKPVNAFNVWKTQRAFSK---YEKSAVLV 396
Cdd:cd00286 263 -------------CDPDHGEAIAALLVIRGPpDLSSKEVERAIARVKETLGHLFSWSPAGVKTGISPKPpaeGEVSVLAL 329

                ...
gi 50592998 397 SNS 399
Cdd:cd00286 330 LNS 332
Tubulin cd06059
The tubulin superfamily and related homologs; The tubulin superfamily includes five distinct ...
2-452 5.12e-122

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: 360.75  E-value: 5.12e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   2 SIVTVQLGQCGNQIGFEVFDAllsdshssqglcsmreneayqasckerffseeengvpiARAVLVDMEPKVINQMLSKaa 81
Cdd:cd06059   1 EIITIQVGQCGNQIGDRFWEL--------------------------------------ARAVLVDMEEGVINEVLKG-- 40
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  82 QSGQWKYGQHACFCQKqGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNLEDQ 161
Cdd:cd06059  41 PLGQLFDPNQFVTGVS-GAGNNWAVGYYVYGPKYIESILDRIRKQVEKCDSLQGFFILHSLGGGTGSGLGSYLLELLEDE 119
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 162 YSNSLKMNQIIWPYGTGE-VIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAK---LMNIKQISFSDINQVLAHQLGS 237
Cdd:cd06059 120 YPKVYRFTFSVFPSPDDDnVITSPYNSVLALNHLTEHADCVLPIDNEALYDICNRqpaTLDIDFPPFDDMNNLVAQLLSS 199
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 238 VFQPTYSAEssfhYRRNPLGDLMEHLVPHPEFKMLSVRNIPHMSENSLayttFTWAGLLKHLRQMLISNAKMEEGIdrhv 317
Cdd:cd06059 200 LTSSLRFEG----SLNVDLNEITTNLVPFPRLHFLLPSLSPLTSANDV----TLEPLTLDQLFSDLFSKDNQLVGC---- 267
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 318 wpplsglpplskmslnkDLHFNTSIANLVILRGKDVQSADVEGFKDPALYTSWLKPVNaFNVWKTQRAFSK---YEKSAV 394
Cdd:cd06059 268 -----------------DPRHGTYLACALLLRGKVFSLSDVRRNIDRIKPKLKFISWN-PDGFKVGLCSVPpvgQKYSLL 329
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 50592998 395 LVSNSQFLVKPLDMIVGKAWNMFASKAYIHQYTKFGIEEEDFLDSFTSLEQVVASYCN 452
Cdd:cd06059 330 FLSNNTSIASTFERLIERFDKLYKRKAFLHHYTGEGMEEGDFSEARESLANLIQEYQE 387
Tubulin pfam00091
Tubulin/FtsZ family, GTPase domain; This family includes the tubulin alpha, beta and gamma ...
2-213 2.55e-68

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: 215.93  E-value: 2.55e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998     2 SIVTVQLGQCGNQIGFEVFDALLSDshssqglcsmreneaYQASCKERFFSEEENGVPIARAVLVDMEPKVINQMLSKaa 81
Cdd:pfam00091   1 EIIVIGVGGAGNNIGNALWELLCLE---------------HGIDSLNVFFSESGSVEFIPRSLAIDTDPQALNEIKAG-- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    82 qsgqwkYGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNLEDQ 161
Cdd:pfam00091  64 ------FNPNKILLGKEGTGGNGAGGYPEIGREAAEESLEEIRKEVEGCDMLQGFFITASLGGGTGSGAAPVIAEILKEL 137
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 50592998   162 YSNSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKIC 213
Cdd:pfam00091 138 YPGALTVAVVTFPFGFSEGVVRPYNAILGLKELIEHSDSVIVIDNDALYDIC 189
epsilon_tubulin cd02190
The epsilon-tubulin family; The tubulin superfamily includes five distinct families, the ...
3-450 7.65e-61

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: 204.78  E-value: 7.65e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   3 IVTVQLGQCGNQIGFEVFDALLSDsHSSQGlcsmrENEAYQASCKERFFSEEENGVPI------------ARAVLVDMEP 70
Cdd:cd02190   3 IITVQVGQCGNQIGCRFWDLALRE-HAAYN-----KDGVYDDSMSSFFRNVDTRSGDPgddggspikslkARAVLIDMEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  71 KVINQMLSkaaqsGQWK--YGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGS 148
Cdd:cd02190  77 GVVNELLK-----GPLGdlFDETQLVTDVSGAGNNWAHGYHEYGPQYGESILEKLRRAAEKCDSLQSFFLLHSLGGGTGS 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 149 GLGAFVTQNLEDQYSNSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNI--------- 219
Cdd:cd02190 152 GLGSYILELLEDEFPDVYRFVTSVFPSGDDDVITSPYNSVLALRELTEHADCVLPVENQALMDIVNKIKSSkdkgktgvl 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 220 -------------KQISFSDINQVLAHQLGSVfqptySAESSFHYRRNPlgDLME---HLVPHPEFKMLsvrniphMSEN 283
Cdd:cd02190 232 aainssgggqkkgKKKPFDDMNNIVANLLLNL-----TSSMRFEGSLNV--DLNEittNLVPFPRLHFL-------LSSL 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 284 SLAYTTFTWAGLLKHLRQMLisnakmeegidRHVWPP---LSGLPPLSkmslnkdlhfNTSIANLVILRGkDVQSAD--- 357
Cdd:cd02190 298 SPLYALADVRLPPRRLDQMF-----------SDAFSRdhqLLKADPKH----------GLYLACALLVRG-NVSISDlrr 355
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 358 -VEGFKDPALYTSWLKpvnafNVWKT---QRAFSKYEKSAVLVSNSQFLVKPLDMIVGKAWNMFASKAYIHQYTKfGIEE 433
Cdd:cd02190 356 nIDRLKRQLKFVSWNQ-----DGWKIglcSVPPVGQPYSLLCLANNTCIKPTFTEMHERFDKLYKRKAHLHHYTQ-YMEQ 429
                       490
                ....*....|....*..
gi 50592998 434 EDFLDSFTSLEQVVASY 450
Cdd:cd02190 430 DDFDEALESLLDLIEEY 446
gamma_tubulin cd02188
The gamma-tubulin family; Gamma-tubulin is a ubiquitous phylogenetically conserved member of ...
3-273 2.22e-60

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: 203.16  E-value: 2.22e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   3 IVTVQLGQCGNQIGFEVFDALLSDsH--SSQGlcSMRENEAYQASCKERFFSEEENGVPIARAVLVDMEPKVINQMlska 80
Cdd:cd02188   3 IITLQVGQCGNQIGSEFWKQLCSE-HgiSPDG--SLEDFATDGNDRKDVFFYQADDEHYIPRAILLDLEPRVINSI---- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  81 aQSGQWK--YGQHACFCQKQGS--GNNWAYGYSvHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQ 156
Cdd:cd02188  76 -QNSPYKnlFNPENIYLSKEGGgaGNNWASGYS-QGEKVQEEILDIIDREAEGSDSLEGFVLCHSIAGGTGSGMGSYLLE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 157 NLEDQYSNSLKMNQIIWP--YGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQISFSDINQ----V 230
Cdd:cd02188 154 RLSDRYPKKLIQTYSVFPnqEESSDVVVQPYNSILTLKRLTLNADCVVVLDNTALNRIATDRLKIDNPSFSQINSlistV 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 50592998 231 LAHQLGSVFQPTYSaessfhyrRNPLGDLMEHLVPHPEFKMLS 273
Cdd:cd02188 234 MSASTSTLRFPGYM--------NNDLVSLISSLIPTPRLHFLM 268
alpha_tubulin cd02186
The alpha-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
3-445 9.15e-56

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: 190.83  E-value: 9.15e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   3 IVTVQLGQCGNQIGFEVFDaLLSDSHSSQGLCSMRENEAYQASCKER--FFSEEENG--VPiaRAVLVDMEPKVINQmls 78
Cdd:cd02186   3 IISIHVGQAGVQIGNACWE-LFCLEHGIQPDGQMPSDKTIGGDDDNFntFFSETGSGkyVP--RAVFVDLEPTVIDE--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  79 kaAQSGQWK--YGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQ 156
Cdd:cd02186  77 --IRTGPYRqlFHPEQLISGKEDAANNFARGYYTIGKEIIDPVLDRIRKLAEQCDGLQGFLIFHSVGGGTGSGLTSLLLE 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 157 NLEDQYSNSLKMNQIIWPYG-TGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQISFSDINQVLAHQL 235
Cdd:cd02186 155 RLSVDYGKKSKLEFSIYPSPqVSTSVVEPYNSVLTTHSLLEHSDCSILLDNEALYDICRRQLDIERPTYTNLNRLIAQVV 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 236 GSVFqptysaeSSFHYRRNPLGDLME---HLVPHPEFKMLSVRNIPHMSENSLAYTTFTwaglLKHLRQMLISNAKMeeg 312
Cdd:cd02186 235 SSLT-------ASLRFDGALNVDLNEfqtNLVPYPRIHFPLVSYAPIISAEKANHEQLS----VQEITNSCFEPANQ--- 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 313 idrhvwpplsglpplskMsLNKDLHFNTSIANLVILRGkDVQSADVEgfkdpalytswlkpvNAFNVWKTQRA------- 385
Cdd:cd02186 301 -----------------M-VKCDPRHGKYMACCLLYRG-DVVPKDVN---------------AAIATIKTKRTiqfvdwc 346
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 386 --------------------FSKYEKSAVLVSNSQFLVKPLDMIVGKAWNMFASKAYIHQYTKFGIEEEDF---LDSFTS 442
Cdd:cd02186 347 ptgfkvginyqpptvvpgsdLAKVDRSVCMLANSTAIAEAFQRLDHKFDLLYSKRAFVHWYVGEGMEEGEFseaREDLAA 426

                ...
gi 50592998 443 LEQ 445
Cdd:cd02186 427 LEK 429
beta_tubulin cd02187
The beta-tubulin family; The tubulin superfamily includes five distinct families, the alpha-, ...
1-452 2.04e-52

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: 182.00  E-value: 2.04e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   1 MSIVTVQLGQCGNQIGfEVFDALLSDSHssqGLCSMRENEAYQASCKER---FFSEEENGVPIARAVLVDMEPKVINQMl 77
Cdd:cd02187   1 REIIHIQIGQCGNQIG-AKFWETISKEH---GIDPDGTYKGDSDLQLERinvYFNEASGGKYVPRAVLVDLEPGTIDSV- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  78 skaaQSGQwkYGQ---HACFCQKQ-GSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAF 153
Cdd:cd02187  76 ----RSGP--YGQlfrPDNFVFGQsGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGLGTL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 154 VTQNLEDQYSNSLKMNQIIWPYG-TGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQISFSDINQVLA 232
Cdd:cd02187 150 LLSKLREEYPDRIMSTFSVLPSPkVSDTVVEPYNAVLSLHQLVENADETFCIDNEALYNICQRTLKLTQPTYDDLNHLIS 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 233 hqlgsvfQPTYSAESSFhyrRNPlGDLME-------HLVPHPEFKMLSVRNIPHMSENSLAYTTFTwaglLKHLRQMLIS 305
Cdd:cd02187 230 -------QVMSGITSSL---RFP-GQLNSdlrklatNLVPFPRLHFLTPGFAPLTSRGSQQYRKLT----VPELTQQLFD 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 306 NAKMEEGIDrhvwpPLSGlpplskmslnkdlHFNTSIAnlvILRGKdVQSADVEG------FKDPALYTSWLKpvNAFNV 379
Cdd:cd02187 295 AKNMMAACD-----PRHG-------------RYLTAAA---IFRGR-ISTKEVDEqmskvqNKNSSYFVEWIP--NNVKT 350
                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50592998 380 WKTQRAFSKYEKSAVLVSNSQFLVKPLDmIVGKAWN-MFASKAYIHQYTKFGIEEEDFLDSFTSLEQVVASYCN 452
Cdd:cd02187 351 SVCDIPPRGLKMSATFIGNSTAIQELFK-RLSEQFTaMFRRKAFLHWYTGEGMDEMEFTEAESNLNDLISEYQQ 423
PTZ00387 PTZ00387
epsilon tubulin; Provisional
3-242 1.58e-49

epsilon tubulin; Provisional


Pssm-ID: 240395 [Multi-domain]  Cd Length: 465  Bit Score: 175.30  E-value: 1.58e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    3 IVTVQLGQCGNQIGFEVFDALLSDsHSSQGlcsmrENEAYQASCKERFFSEEENGVPI------ARAVLVDMEPKVINQM 76
Cdd:PTZ00387   4 IVTVQVGQCGNQLGHRFWDVALKE-HKKIN-----ANPQYDDARDSFFENVSENVNRPgkenlkARAVLVDMEEGVLNQI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   77 LSKAAQSgqwKYGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQ 156
Cdd:PTZ00387  78 LKSPLGD---LFDENFFVSDVSGAGNNWAVGHMEYGDKYIDSISESVRRQVEQCDSLQSFFLMHSLGGGTGSGLGTRILG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  157 NLEDQYSNSLKMNQIIWPYGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKIC--AKLMNIKQISFSDINQVLAHQ 234
Cdd:PTZ00387 155 MLEDEFPHVFRFCPVVFPSAVDDVITSPYNSFFALRELIEHADCVLPLDNDALANIAdsALSRKKKKLAKGNIKRGPQPH 234

                 ....*...
gi 50592998  235 LGSVFQPT 242
Cdd:PTZ00387 235 KYSVAKPT 242
PTZ00010 PTZ00010
tubulin beta chain; Provisional
3-450 1.01e-45

tubulin beta chain; Provisional


Pssm-ID: 240228 [Multi-domain]  Cd Length: 445  Bit Score: 164.56  E-value: 1.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    3 IVTVQLGQCGNQIGFEVFDALlSDSHSSQGLCSMRENEAYQASCKERFFSEEENGVPIARAVLVDMEPKVINQMlsKAAQ 82
Cdd:PTZ00010   4 IVHIQAGQCGNQIGSKFWEVI-SDEHGIDPTGTYQGDSDLQLERINVYYNEATGGRYVPRAVLMDLEPGTMDSV--RAGP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   83 SGQWKYGQHACFCQkQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNLEDQY 162
Cdd:PTZ00010  81 YGQLFRPDNFIFGQ-SGAGNNWAKGHYTEGAELIDSVLDVVRKEAESCDCLQGFQITHSLGGGTGSGMGTLLISKLREEY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  163 SNSLKMNQIIWPY-GTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQISFSDINQVLAHQLGSVfqp 241
Cdd:PTZ00010 160 PDRIMMTFSVFPSpKVSDTVVEPYNATLSVHQLVENADESMCIDNEALYDICFRTLKLTTPTYGDLNHLVSAVMSGV--- 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  242 tySAESSFHYRRNP-LGDLMEHLVPHPEFKMLSVRNIPHMSENSLAYTTFTWAGLLKhlrQMLisNAKmeegidrhvwpp 320
Cdd:PTZ00010 237 --TCCLRFPGQLNSdLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVPELTQ---QMF--DAK------------ 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  321 lsglpplsKMSLNKDLHFNTSIANLVILRGK------DVQSADVEGfKDPALYTSWLKpvNAFNVWKTQRAFSKYEKSAV 394
Cdd:PTZ00010 298 --------NMMCAADPRHGRYLTASALFRGRmstkevDEQMLNVQN-KNSSYFVEWIP--NNIKSSVCDIPPKGLKMSVT 366
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 50592998  395 LVSNSQFLVKPLDMIVGKAWNMFASKAYIHQYTKFGIEEEDFLDSFTSLEQVVASY 450
Cdd:PTZ00010 367 FIGNSTAIQEMFRRVGEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEY 422
PLN00222 PLN00222
tubulin gamma chain; Provisional
3-267 1.11e-45

tubulin gamma chain; Provisional


Pssm-ID: 215108 [Multi-domain]  Cd Length: 454  Bit Score: 164.63  E-value: 1.11e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    3 IVTVQLGQCGNQIGFEVFDAL-LSDSHSSQGLCsmRENEAYQASCKERFFSEEENGVPIARAVLVDMEPKVINQMlskaa 81
Cdd:PLN00222   5 IITLQVGQCGNQIGMEFWKQLcLEHGISKDGIL--EDFATQGGDRKDVFFYQADDEHYIPRALLIDLEPRVINGI----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   82 QSGQWK--YGQHACFCQKQG--SGNNWAYGYSvHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQN 157
Cdd:PLN00222  78 QNSEYRnlYNHENIFVSDHGggAGNNWASGYH-QGEQVEEDIMDMIDREADGSDSLEGFVLCHSIAGGTGSGMGSYLLEA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  158 LEDQYSNSLKMNQIIWP--YGTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQISFSDINQVLAhql 235
Cdd:PLN00222 157 LNDRYSKKLVQTYSVFPnqMETSDVVVQPYNSLLTLKRLTLNADCVVVLDNTALNRIAVDRLHLENPTFAQTNSLVS--- 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 50592998  236 gSVFQPTYSAESSFHYRRNPLGDLMEHLVPHP 267
Cdd:PLN00222 234 -TVMSASTTTLRYPGYMNNDLVGLLASLIPTP 264
PTZ00335 PTZ00335
tubulin alpha chain; Provisional
3-436 1.27e-40

tubulin alpha chain; Provisional


Pssm-ID: 185562 [Multi-domain]  Cd Length: 448  Bit Score: 150.63  E-value: 1.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    3 IVTVQLGQCGNQIGFEVFDaLLSDSHSSQGLCSMRE--NEAYQASCKERFFSEEENGVPIARAVLVDMEPKVINQMlska 80
Cdd:PTZ00335   4 VISIHIGQAGIQVGNACWE-LFCLEHGIQPDGQMPSdkNIGVEDDAFNTFFSETGAGKHVPRCVFLDLEPTVIDEV---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   81 aQSGQWK--YGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNL 158
Cdd:PTZ00335  79 -RTGTYRqlFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFHAVGGGTGSGLGSLLLERL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  159 EDQYSNSLKMNQIIWPY-GTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQISFSDINQVLAHQLGS 237
Cdd:PTZ00335 158 SVDYGKKSKLGFTIYPSpQVSTAVVEPYNSVLSTHSLLEHTDVAVMLDNEAIYDICRRNLDIERPTYTNLNRLIAQVISS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  238 VfqptySAESSFHYRRN-PLGDLMEHLVPHPEFK-MLSvrniphmsenslAYTTFTWAGLLKHlRQML---ISNAKMEEg 312
Cdd:PTZ00335 238 L-----TASLRFDGALNvDLTEFQTNLVPYPRIHfMLS------------SYAPIISAEKAYH-EQLSvaeITNSAFEP- 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  313 idrhvwpplsglpplSKMSLNKDLHFNTSIANLVILRGkDVQSADVEgfkdpalytswlkpvNAFNVWKTQRA------- 385
Cdd:PTZ00335 299 ---------------ANMMAKCDPRHGKYMACCLMYRG-DVVPKDVN---------------AAIATIKTKRTiqfvdwc 347
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50592998  386 --------------------FSKYEKSAVLVSNSQFLVKPLDMIVGKAWNMFASKAYIHQYTKFGIEEEDF 436
Cdd:PTZ00335 348 ptgfkcginyqpptvvpggdLAKVQRAVCMISNSTAIAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEF 418
Tubulin smart00864
Tubulin/FtsZ family, GTPase domain; This domain is found in all tubulin chains, as well as the ...
47-238 3.04e-40

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: 142.63  E-value: 3.04e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998     47 KERFFSEEeNGVPiaRAVLVDMEPKVINQMLSKaaqsgqwKYGQH----ACFCQKQGSGNNWAYGYSV-----HGPRHEE 117
Cdd:smart00864   1 KIKVFGVG-GGGP--NAVNVDLEPGVIDGVRAN-------TDAQAlnpeSLASGKIQAGNNWTRGLGAgadpeVGREAAE 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    118 SIMNIIRKEVEKCDsfsGFFIIMSMAGGTGSGLGAFVTQNLEDQysNSLKMNQIIWPyGTGEVIVQNYNSILTLSHLYRS 197
Cdd:smart00864  71 ESLDEIREELEGAD---GVFITAGMGGGTGTGAAPVIAEIAKEY--GILTVAVVTKP-FSFEGVVRPYNAELGLEELREH 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 50592998    198 SDALLLHENDAIHKICAKLmNIKQISFSDINQVLAHQLGSV 238
Cdd:smart00864 145 VDSLIVIDNDALLDICGRK-LPLRPAFKDANDLLAQAVSGI 184
PLN00220 PLN00220
tubulin beta chain; Provisional
3-450 5.81e-36

tubulin beta chain; Provisional


Pssm-ID: 215107 [Multi-domain]  Cd Length: 447  Bit Score: 138.03  E-value: 5.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    3 IVTVQLGQCGNQIGFEvFDALLSDSHSSQGLCSMRENEAYQASCKERFFSEEENGVPIARAVLVDMEPKVINqmlskAAQ 82
Cdd:PLN00220   4 ILHIQGGQCGNQIGAK-FWEVVCDEHGIDPTGTYHGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMD-----SVR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   83 SGqwKYGQ-----HACFCQkQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQN 157
Cdd:PLN00220  78 SG--PYGQifrpdNFVFGQ-SGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  158 LEDQYSNSLKMNQIIWPY-GTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQISFSDINQVLAHQLG 236
Cdd:PLN00220 155 IREEYPDRMMLTFSVFPSpKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLTTPSFGDLNHLISATMS 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  237 SVfqptySAESSFHYRRNP-LGDLMEHLVPHPEFKMLSVRNIPHMSENSLAYTTFTWAGLLKhlrQMLISNAKMEEGIDR 315
Cdd:PLN00220 235 GV-----TCCLRFPGQLNSdLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRALTVPELTQ---QMWDAKNMMCAADPR 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  316 HVwpplsglpplskmslnkdlHFNTSIAnlvILRGK------DVQSADVEGfKDPALYTSWLKpvNAFNVWKTQRAFSKY 389
Cdd:PLN00220 307 HG-------------------RYLTASA---MFRGKmstkevDEQMINVQN-KNSSYFVEWIP--NNVKSSVCDIPPKGL 361
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50592998  390 EKSAVLVSNSQFLVKPLDMIVGKAWNMFASKAYIHQYTKFGIEEEDFLDSFTSLEQVVASY 450
Cdd:PLN00220 362 KMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEY 422
PLN00221 PLN00221
tubulin alpha chain; Provisional
3-436 3.16e-26

tubulin alpha chain; Provisional


Pssm-ID: 177802  Cd Length: 450  Bit Score: 110.28  E-value: 3.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998    3 IVTVQLGQCGNQIG---FEVF---DALLSDSHSSQGLCSMRENEAYQAsckerFFSEEENGVPIARAVLVDMEPKVINQM 76
Cdd:PLN00221   4 CISIHIGQAGIQVGnacWELYcleHGIQPDGQMPSDKTVGGGDDAFNT-----FFSETGAGKHVPRAVFVDLEPTVIDEV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998   77 lskaaQSGQWK--YGQHACFCQKQGSGNNWAYGYSVHGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFV 154
Cdd:PLN00221  79 -----RTGTYRqlFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  155 TQNLEDQYSNSLKMNQIIWPY-GTGEVIVQNYNSILTLSHLYRSSDALLLHENDAIHKICAKLMNIKQISFSDINQVLAH 233
Cdd:PLN00221 154 LERLSVDYGKKSKLGFTVYPSpQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQ 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  234 QLGSVfqptySAESSFHYRRN-PLGDLMEHLVPHPEFK-MLSvrniphmsenSLAYTTFTWAGLLKHLRQMLISNAKMEe 311
Cdd:PLN00221 234 VISSL-----TASLRFDGALNvDITEFQTNLVPYPRIHfMLS----------SYAPVISAEKAYHEQLSVAEITNSAFE- 297
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998  312 gidrhvwpplsglpPLSKMSLNKDLHfNTSIANLVILRG----KDVQSADVE---------------GFKDPALYtswlK 372
Cdd:PLN00221 298 --------------PASMMAKCDPRH-GKYMACCLMYRGdvvpKDVNAAVATiktkrtiqfvdwcptGFKCGINY----Q 358
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50592998  373 P---VNAFNVWKTQRAfskyeksAVLVSNSQFLVKPLDMIVGKAWNMFASKAYIHQYTKFGIEEEDF 436
Cdd:PLN00221 359 PptvVPGGDLAKVQRA-------VCMISNSTAVAEVFSRIDHKFDLMYAKRAFVHWYVGEGMEEGEF 418
misato cd06060
Misato segment II tubulin-like domain; Human Misato shows similarity with Tubulin/FtsZ family ...
102-199 9.80e-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: 47.70  E-value: 9.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 102 NNWAYGYSV-HGPRHEESIMNIIRKEVEKCDSFSGFFIIMSMAGGtGSGLGAFVTQNLEDQYSNSlkmnqIIWPYGTGEV 180
Cdd:cd06060 175 DNFSQGEELfSDLEELEEFEDRLRFFVEECDSLQGFQILVDTDDG-FGGVAAKLLENLRDEYGKK-----SILTPGLSPA 248
                        90       100
                ....*....|....*....|....*....
gi 50592998 181 ----------IVQNYNSILTLSHLYRSSD 199
Cdd:cd06060 249 sppdpdsqrrIKRLLNDALSLSSLSEHSS 277
CetZ_tubulin-like cd02202
Cell-structure-related euryarchaeota tubulin/FtsZ homologs; CetZ proteins comprise a distinct ...
116-247 8.67e-04

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: 41.46  E-value: 8.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 116 EESIMNIIR--KEVEKCDsFSGFFIIMSMAGGTGSGLGAFVTQNLEDQYsNSLKMNQIIWPYGTGEVIVQnYNSILTLSH 193
Cdd:cd02202  80 EEDIDELLRalDTAPFSE-ADAFLVVAGLGGGTGSGAAPVLAEELKERY-DKPVYALGVLPAAEEGGRYA-LNAARSLRS 156
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 194 LYRSSDALLLHENDAIHKICAKLmnikQISFSDINQVLAHQLGSVF------QPTYSAES 247
Cdd:cd02202 157 LVELADAVILFDNDAWRRSGESI----AEAYDRINEEIAERLGALLaagevdAPKSVGES 212
FtsZ_CetZ-like cd02191
Subfamily of FitZ and Cell-structure-related euryarchaeota tubulin/FtsZ homolog-like; FtsZ is ...
123-236 1.32e-03

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: 40.62  E-value: 1.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50592998 123 IRKEVEKCDSFSGFFIIMSMAGGTGSGLGAFVTQNLEDQYSnslkmnQIIWPYGT------GEVIVQnyNSILTLSHLYR 196
Cdd:cd02191  83 IMEALEGRVEADMIFVTTGLGGGTGSGGAPVLAEALKKVYD------VLTVAVVTlpfadeGALYMQ--NAGEGLRTLAE 154
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 50592998 197 SSDALLLHENDAIHKICAKLMNikqiSFSDINQVLAHQLG 236
Cdd:cd02191 155 EADALILVDNEKLRSIGGSLSE----AYDAINEVLARRVG 190
 
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