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Conserved domains on  [gi|73920151|sp|Q6ZT98|]
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RecName: Full=Tubulin polyglutamylase TTLL7; AltName: Full=Testis development protein NYD-SP30; AltName: Full=Tubulin--tyrosine ligase-like protein 7

Protein Classification

tubulin--tyrosine ligase family protein( domain architecture ID 10504173)

tubulin--tyrosine ligase (TTL) family protein such as TTL that catalyzes the post-translational retyrosination of detyrosinated a-tubulin, and TTL-like (TTLL) enzymes that catalyze the glycylation and/or glutamylation, the post-translational addition of glycines and glutamates to genetically encoded glutamates in the intrinsically disordered tubulin C-terminal tails

CATH:  3.30.470.20
EC:  6.3.2.-
Gene Ontology:  GO:0005524
PubMed:  9538689|23358242|10685598|15890843

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 91-376 9.69e-78

Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.


:

Pssm-ID: 397308  Cd Length: 291  Bit Score: 254.18  E-value: 9.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151    91 NYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYvkelKKKRKQKTFIVKPANGAMGHGI 170
Cdd:pfam03133   7 YHQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKGDFLPRTFILPTDLAEFVDY----FEDRERNTWIVKPSASARGRGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151   171 SLIRNGDKLP--SQD-HLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPnESNLTQLYMH 247
Cdd:pfam03133  83 RVTNKLSQIPkwSQSrPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPS-SSDLDDVEMH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151   248 LTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQanQHDVAKFWSDISELVVKTLIVAEphvlhaYRMCRPGQPPGSEs 327
Cdd:pfam03133 162 LTNYSIQKKSSSLNEDYNEPHGHKWSLQNFWKYLE--EKDKDEIWLEIESIIIKTILAAE------VEASRLNVQPLPN- 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 73920151   328 vCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALK 376
Cdd:pfam03133 233 -CFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLN 280
YhaN super family cl34808
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
384-474 9.25e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


The actual alignment was detected with superfamily member COG4717:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 9.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151 384 DKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSD---WEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIypp 460
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDeeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--- 471

                        90
                ....*....|....
gi 73920151 461 edKALLEKYENLLA 474
Cdd:COG4717 472 --AELLQELEELKA 483
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 91-376 9.69e-78

Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.


Pssm-ID: 397308  Cd Length: 291  Bit Score: 254.18  E-value: 9.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151    91 NYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYvkelKKKRKQKTFIVKPANGAMGHGI 170
Cdd:pfam03133   7 YHQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKGDFLPRTFILPTDLAEFVDY----FEDRERNTWIVKPSASARGRGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151   171 SLIRNGDKLP--SQD-HLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPnESNLTQLYMH 247
Cdd:pfam03133  83 RVTNKLSQIPkwSQSrPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPS-SSDLDDVEMH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151   248 LTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQanQHDVAKFWSDISELVVKTLIVAEphvlhaYRMCRPGQPPGSEs 327
Cdd:pfam03133 162 LTNYSIQKKSSSLNEDYNEPHGHKWSLQNFWKYLE--EKDKDEIWLEIESIIIKTILAAE------VEASRLNVQPLPN- 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 73920151   328 vCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALK 376
Cdd:pfam03133 233 -CFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLN 280
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 128-209 1.16e-05

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 48.01  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151 128 VPRTWIF--PAEYTQFQNYVKElkkkrkqkTFIVKPANGAMGHGISLIRNGDKLPS---------QDHLIVQEYIEKPfl 196
Cdd:COG0189 111 VPPTLVTrdPDDLRAFLEELGG--------PVVLKPLDGSGGRGVFLVEDEDALESilealtelgSEPVLVQEFIPEE-- 180

                        90
                ....*....|...
gi 73920151 197 mEGykFDLRIYIL 209
Cdd:COG0189 181 -DG--RDIRVLVV 190
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
384-474 9.25e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 9.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151 384 DKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSD---WEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIypp 460
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDeeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--- 471

                        90
                ....*....|....
gi 73920151 461 edKALLEKYENLLA 474
Cdd:COG4717 472 --AELLQELEELKA 483
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 380-447 1.63e-03

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269866  Cd Length: 70  Bit Score: 37.65  E-value: 1.63e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73920151 380 IRTSDKRRNLakqkaeaQRRLYGQN-SIKRLlpgssdweQQRHQLERRKEELKERLAQVRKQISREEHE 447
Cdd:cd14718   5 IRLKQKRRTL-------KNRGYAQScRSKRV--------QQRHVLESEKCQLQQQVEQLKQEVSRLARE 58
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 384-502 5.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151    384 DKRRNLAKQKAEAQRRLYG---------------QNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQIS-----R 443
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYAlaneisrleqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeeL 353

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73920151    444 EEHENRHmgnyrriypPEDKALLEKYENLLAVAFQTFLSGRAASFQRE-----LNNPLKRMKEE 502
Cdd:TIGR02168  354 ESLEAEL---------EELEAELEELESRLEELEEQLETLRSKVAQLElqiasLNNEIERLEAR 408
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 158-194 9.26e-03

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 38.87  E-value: 9.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 73920151   158 IVKPANGAMGHGISLIRNGDKL-----------PSQDHLIVQEYIEKP 194
Cdd:TIGR00768 127 VLKPVFGSWGRGVSLARDRQAAesllehfeqlnGPQNLFLVQEYIKKP 174
 
Name Accession Description Interval E-value
TTL pfam03133
Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several ...
 91-376 9.69e-78

Tubulin-tyrosine ligase family; Tubulins and microtubules are subjected to several post-translational modifications of which the reversible detyrosination/tyrosination of the carboxy-terminal end of most alpha-tubulins has been extensively analysed. This modification cycle involves a specific carboxypeptidase and the activity of the tubulin-tyrosine ligase (TTL). The true physiological function of TTL has so far not been established. Tubulin-tyrosine ligase (TTL) catalyzes the ATP-dependent post-translational addition of a tyrosine to the carboxy terminal end of detyrosinated alpha-tubulin. In normally cycling cells, the tyrosinated form of tubulin predominates. However, in breast cancer cells, the detyrosinated form frequently predominates, with a correlation to tumour aggressiveness. On the other hand, 3-nitrotyrosine has been shown to be incorporated, by TTL, into the carboxy terminal end of detyrosinated alpha-tubulin. This reaction is not reversible by the carboxypeptidase enzyme. Cells cultured in 3-nitrotyrosine rich medium showed evidence of altered microtubule structure and function, including altered cell morphology, epithelial barrier dysfunction, and apoptosis. Bacterial homologs of TTL are predicted to form peptide tags. Some of these are fused to a 2-oxoglutarate Fe(II)-dependent dioxygenase domain.


Pssm-ID: 397308  Cd Length: 291  Bit Score: 254.18  E-value: 9.69e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151    91 NYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYvkelKKKRKQKTFIVKPANGAMGHGI 170
Cdd:pfam03133   7 YHQALNHFPGSYEITRKDLLWKNIKRTPCDRGLKGDFLPRTFILPTDLAEFVDY----FEDRERNTWIVKPSASARGRGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151   171 SLIRNGDKLP--SQD-HLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPnESNLTQLYMH 247
Cdd:pfam03133  83 RVTNKLSQIPkwSQSrPLVVQKYIERPLLIDGRKFDIRLYVLVTSVNPLRVYVYREGLLRFASVKYSPS-SSDLDDVEMH 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151   248 LTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQanQHDVAKFWSDISELVVKTLIVAEphvlhaYRMCRPGQPPGSEs 327
Cdd:pfam03133 162 LTNYSIQKKSSSLNEDYNEPHGHKWSLQNFWKYLE--EKDKDEIWLEIESIIIKTILAAE------VEASRLNVQPLPN- 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 73920151   328 vCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALK 376
Cdd:pfam03133 233 -CFELYGFDFMIDENLKPWLLEVNSSPSLHSTTKLDARLKEQLIDDVLN 280
LysX COG0189
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
 128-209 1.16e-05

Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 439959 [Multi-domain]  Cd Length: 289  Bit Score: 48.01  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151 128 VPRTWIF--PAEYTQFQNYVKElkkkrkqkTFIVKPANGAMGHGISLIRNGDKLPS---------QDHLIVQEYIEKPfl 196
Cdd:COG0189 111 VPPTLVTrdPDDLRAFLEELGG--------PVVLKPLDGSGGRGVFLVEDEDALESilealtelgSEPVLVQEFIPEE-- 180

                        90
                ....*....|...
gi 73920151 197 mEGykFDLRIYIL 209
Cdd:COG0189 181 -DG--RDIRVLVV 190
ATP-grasp_3 pfam02655
ATP-grasp domain; No functional information or experimental verification of function is known ...
 156-192 5.15e-04

ATP-grasp domain; No functional information or experimental verification of function is known in this family. This family appears to be an ATP-grasp domain (Pers. obs. A Bateman).


Pssm-ID: 396979 [Multi-domain]  Cd Length: 160  Bit Score: 41.60  E-value: 5.15e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 73920151   156 TFIVKPANGAMGHGISLIRNGDKL-PSQDHLIVQEYIE 192
Cdd:pfam02655  33 KYVVKPRDGCGGEGVRKVENGREDeAFIENVLVQEFIE 70
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
384-474 9.25e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 9.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151 384 DKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSD---WEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIypp 460
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDeeeLEEELEELEEELEELEEELEELREELAELEAELEQLEEDGEL--- 471

                        90
                ....*....|....
gi 73920151 461 edKALLEKYENLLA 474
Cdd:COG4717 472 --AELLQELEELKA 483
bZIP_Maf_large cd14718
Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a ...
 380-447 1.63e-03

Basic leucine zipper (bZIP) domain of large musculoaponeurotic fibrosarcoma (Maf) proteins: a DNA-binding and dimerization domain; Maf proteins are Basic leucine zipper (bZIP) transcription factors that may participate in the activator protein-1 (AP-1) complex, which is implicated in many cell functions including proliferation, apoptosis, survival, migration, tumorigenesis, and morphogenesis, among others. Maf proteins fall into two groups: small and large. The large Mafs (c-Maf, MafA, MafB, and neural retina leucine zipper or NRL) contain an N-terminal transactivation domain, a linker region of varying size, an anxillary DNA-binding domain, a C-terminal bZIP domain. They function as critical regulators of terminal differentiation in the blood and in many tissues such as bone, brain, kidney, pancreas, and retina. MafA and MafB also play crucial roles in islet beta cells; they regulate genes essential for glucose sensing and insulin secretion cooperatively and sequentially. Large Mafs are also implicated in oncogenesis; MafB and c-Maf chromosomal translocations result in multiple myelomas. bZIP factors act in networks of homo and heterodimers in the regulation of a diverse set of cellular processes. The bZIP structural motif contains a basic region and a leucine zipper, composed of alpha helices with leucine residues 7 amino acids apart, which stabilize dimerization with a parallel leucine zipper domain. Dimerization of leucine zippers creates a pair of the adjacent basic regions that bind DNA and undergo conformational change. Dimerization occurs in a specific and predictable manner resulting in hundreds of dimers having unique effects on transcription.


Pssm-ID: 269866  Cd Length: 70  Bit Score: 37.65  E-value: 1.63e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 73920151 380 IRTSDKRRNLakqkaeaQRRLYGQN-SIKRLlpgssdweQQRHQLERRKEELKERLAQVRKQISREEHE 447
Cdd:cd14718   5 IRLKQKRRTL-------KNRGYAQScRSKRV--------QQRHVLESEKCQLQQQVEQLKQEVSRLARE 58
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 415-531 5.20e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 39.71  E-value: 5.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151 415 DWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAvafqtflsgraasfqrelNN 494
Cdd:COG4026 146 EIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLK------------------KR 207

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 73920151 495 PLKRMKEEDILDLLEQCEIDDEKLMGKTTKTRGPKPL 531
Cdd:COG4026 208 LLEVFSLEELWKELFPEELPEEDFIYFATENLKPGKI 244
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 384-502 5.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 5.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 73920151    384 DKRRNLAKQKAEAQRRLYG---------------QNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQIS-----R 443
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYAlaneisrleqqkqilRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEelkeeL 353

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 73920151    444 EEHENRHmgnyrriypPEDKALLEKYENLLAVAFQTFLSGRAASFQRE-----LNNPLKRMKEE 502
Cdd:TIGR02168  354 ESLEAEL---------EELEAELEELESRLEELEEQLETLRSKVAQLElqiasLNNEIERLEAR 408
rimK_fam TIGR00768
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ...
 158-194 9.26e-03

alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).


Pssm-ID: 273261 [Multi-domain]  Cd Length: 276  Bit Score: 38.87  E-value: 9.26e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 73920151   158 IVKPANGAMGHGISLIRNGDKL-----------PSQDHLIVQEYIEKP 194
Cdd:TIGR00768 127 VLKPVFGSWGRGVSLARDRQAAesllehfeqlnGPQNLFLVQEYIKKP 174
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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