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Conserved domains on  [gi|113951751|ref|NP_001039316|]
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aminoacyl tRNA synthase complex-interacting multifunctional protein 1a [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02610 super family cl33529
probable methionyl-tRNA synthetase
 107-315 9.53e-87

probable methionyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02610:

Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 276.28  E-value: 9.53e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 107 VSASPSAASTKTPSAKNNDEAKKMKAEKKGEKKEKKAAAPPQEDAKVDVSRLDLRVGRIISAEKHPDADSLYVEQVDVGE 186
Cdd:PLN02610 592 AARAEAAEAKKLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGE 671

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 187 AAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCASSPE--KVEILDPPSGAAAGDRITFQGFPGEPD 264
Cdd:PLN02610 672 GAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDhtKVELVEPPESAAVGERVTFPGFEGEPD 751

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 113951751 265 KELNPKKKVWEQVQPDLLTDDQCVATYKGVAFeVTGKGVCKAQTMSKSGIK 315
Cdd:PLN02610 752 DVLNPKKKVWETLQPDLHTNSELVACYKDVPF-TTSAGVCKVASIANGSIR 801
ATP-synt_Fo_b super family cl21478
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 5-81 1.32e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


The actual alignment was detected with superfamily member PRK08476:

Pssm-ID: 473877 [Multi-domain]  Cd Length: 141  Bit Score: 38.52  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113951751   5 RSLFKMSGHTPSLMRLEqkaAEAEQIIEYLKQQVQLLKEKAIVQATLKEEKKLMVENAKLKKDIEELKKQLLDKEKM 81
Cdd:PRK08476  45 NDLEKVKTNSSDVSEIE---HEIETILKNAREEANKIRQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQE 118
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 107-315 9.53e-87

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 276.28  E-value: 9.53e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 107 VSASPSAASTKTPSAKNNDEAKKMKAEKKGEKKEKKAAAPPQEDAKVDVSRLDLRVGRIISAEKHPDADSLYVEQVDVGE 186
Cdd:PLN02610 592 AARAEAAEAKKLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGE 671

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 187 AAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCASSPE--KVEILDPPSGAAAGDRITFQGFPGEPD 264
Cdd:PLN02610 672 GAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDhtKVELVEPPESAAVGERVTFPGFEGEPD 751

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 113951751 265 KELNPKKKVWEQVQPDLLTDDQCVATYKGVAFeVTGKGVCKAQTMSKSGIK 315
Cdd:PLN02610 752 DVLNPKKKVWETLQPDLHTNSELVACYKDVPF-TTSAGVCKVASIANGSIR 801
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 153-255 8.27e-63

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.


Pssm-ID: 239198 [Multi-domain]  Cd Length: 105  Bit Score: 193.98  E-value: 8.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 153 VDVSRLDLRVGRIISAEKHPDADSLYVEQVDVGEAAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMC 232
Cdd:cd02799    1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                         90       100
                 ....*....|....*....|....*
gi 113951751 233 ASSP--EKVEILDPPSGAAAGDRIT 255
Cdd:cd02799   81 ASNAdhEKVELLEPPEGAKPGERVT 105
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 160-253 3.45e-37

Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.


Pssm-ID: 396251 [Multi-domain]  Cd Length: 96  Bit Score: 128.13  E-value: 3.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751  160 LRVGRIISAEKHPDADSLYVEQVDVGEAAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCAS--SPE 237
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEelDGG 80

                          90
                  ....*....|....*.
gi 113951751  238 KVEILDPPSGAAAGDR 253
Cdd:pfam01588  81 SVGLLEPPADVPPGTK 96
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
154-252 1.23e-20

tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 92.22  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 154 DVSRLD-LRVGRIISAEKHPDADSLYVEQVDVGEaAPRTVVSGLVKH----IPLDQMQNRMAVLLCNLKPAKMRGVLSQA 228
Cdd:COG0073   37 KVGGLDgLRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGAPNVyagdKVPEALVGAQVPGVVNLKPRKIRGVESEG 115

                         90       100
                 ....*....|....*....|....*...
gi 113951751 229 MVMCASSPEKVE----ILDPPSGAAAGD 252
Cdd:COG0073  116 MLCSAEELGLGEdhdgILELPEDAPPGD 143
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 154-254 2.04e-19

methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273059 [Multi-domain]  Cd Length: 137  Bit Score: 82.86  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751  154 DVSRLDLRVGRIISAEKHPDADSLYVEQVDVGEAApRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCA 233
Cdd:TIGR00399  36 DFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEK-RQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAA 114

                          90       100
                  ....*....|....*....|..
gi 113951751  234 SSPEKV-EILDPPSGAAAGDRI 254
Cdd:TIGR00399 115 EDDGKVlFLLSPDQEAIAGERI 136
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 5-81 1.32e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 38.52  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113951751   5 RSLFKMSGHTPSLMRLEqkaAEAEQIIEYLKQQVQLLKEKAIVQATLKEEKKLMVENAKLKKDIEELKKQLLDKEKM 81
Cdd:PRK08476  45 NDLEKVKTNSSDVSEIE---HEIETILKNAREEANKIRQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQE 118
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
 20-75 2.27e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 38.32  E-value: 2.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113951751   20 LEQKAAEAEQIIEYLKQQVQLLK------EKAIVQATLKEEKKLMVENAKLKKDIEELKKQL 75
Cdd:pfam10211 124 LEKKIADLEEEKEELEKQVAELKakceaiEKREEERRQAEEKKHAEEIAFLKKTNQQLKAQL 185
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 107-315 9.53e-87

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 276.28  E-value: 9.53e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 107 VSASPSAASTKTPSAKNNDEAKKMKAEKKGEKKEKKAAAPPQEDAKVDVSRLDLRVGRIISAEKHPDADSLYVEQVDVGE 186
Cdd:PLN02610 592 AARAEAAEAKKLAKQLKKKALSDGGKKKQGKKAGGGGKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGE 671

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 187 AAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCASSPE--KVEILDPPSGAAAGDRITFQGFPGEPD 264
Cdd:PLN02610 672 GAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMRGIKSQAMVLAASNSDhtKVELVEPPESAAVGERVTFPGFEGEPD 751

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 113951751 265 KELNPKKKVWEQVQPDLLTDDQCVATYKGVAFeVTGKGVCKAQTMSKSGIK 315
Cdd:PLN02610 752 DVLNPKKKVWETLQPDLHTNSELVACYKDVPF-TTSAGVCKVASIANGSIR 801
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 153-255 8.27e-63

tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of tRNA binding proteins, including Caenorhabditis elegans methionyl-tRNA synthetase (CeMetRS), human tyrosyl- tRNA synthetase (hTyrRS), Saccharomyces cerevisiae Arc1p, human p43 and EMAP2. CeMetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. A EMAP-II-like cytokine also is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain.


Pssm-ID: 239198 [Multi-domain]  Cd Length: 105  Bit Score: 193.98  E-value: 8.27e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 153 VDVSRLDLRVGRIISAEKHPDADSLYVEQVDVGEAAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMC 232
Cdd:cd02799    1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                         90       100
                 ....*....|....*....|....*
gi 113951751 233 ASSP--EKVEILDPPSGAAAGDRIT 255
Cdd:cd02799   81 ASNAdhEKVELLEPPEGAKPGERVT 105
tRNA_bindingDomain cd02153
The tRNA binding domain is also known as the Myf domain in literature. This domain is found in ...
 160-254 2.21e-39

The tRNA binding domain is also known as the Myf domain in literature. This domain is found in a diverse collection of tRNA binding proteins, including prokaryotic phenylalanyl tRNA synthetases (PheRS), methionyl-tRNA synthetases (MetRS), human tyrosyl-tRNA synthetase(hTyrRS), Saccharomyces cerevisiae Arc1p, Thermus thermophilus CsaA, Aquifex aeolicus Trbp111, human p43 and human EMAP-II. PheRS, MetRS and hTyrRS aminoacylate their cognate tRNAs. Arc1p is a transactivator of yeast methionyl-tRNA and glutamyl-tRNA synthetases. The molecular chaperones Trbp111 and CsaA also contain this domain. CsaA has export related activities; Trbp111 is structure-specific recognizing the L-shape of the tRNA fold. This domain has general tRNA binding properties. In a subset of this family this domain has the added capability of a cytokine. For example the p43 component of the Human aminoacyl-tRNA synthetase complex is cleaved to release EMAP-II cytokine. EMAP-II has multiple activities during apoptosis, angiogenesis and inflammation and participates in malignant transformation. An EMAP-II-like cytokine is released from hTyrRS upon cleavage. The active cytokine heptapeptide locates to this domain. For homodimeric members of this group which include CsaA, Trbp111 and Escherichia coli MetRS this domain acts as a dimerization domain.


Pssm-ID: 239066 [Multi-domain]  Cd Length: 99  Bit Score: 133.80  E-value: 2.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 160 LRVGRIISAEKHPDADSLYVEQVDVGEAAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCAS----S 235
Cdd:cd02153    1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEelglE 80

                         90
                 ....*....|....*....
gi 113951751 236 PEKVEILDPPSGAAAGDRI 254
Cdd:cd02153   81 EGSVGILELPEDAPVGDRI 99
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 160-253 3.45e-37

Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, prokaryotic phenylalanyl tRNA synthetases the yeast GU4 nucleic-binding protein (G4p1 or p42, ARC1), human tyrosyl-tRNA synthetase, and endothelial-monocyte activating polypeptide II. G4p1 binds specifically to tRNA form a complex with methionyl-tRNA synthetases. In human tyrosyl-tRNA synthetase this domain may direct tRNA to the active site of the enzyme. This domain may perform a common function in tRNA aminoacylation.


Pssm-ID: 396251 [Multi-domain]  Cd Length: 96  Bit Score: 128.13  E-value: 3.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751  160 LRVGRIISAEKHPDADSLYVEQVDVGEAAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCAS--SPE 237
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEelDGG 80

                          90
                  ....*....|....*.
gi 113951751  238 KVEILDPPSGAAAGDR 253
Cdd:pfam01588  81 SVGLLEPPADVPPGTK 96
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 154-254 5.45e-29

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 116.79  E-value: 5.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 154 DVSRLDLRVGRIISAEKHPDADSLYVEQVDVGEAaPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCA 233
Cdd:PRK00133 572 DFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGEE-TRQVFSGIKSAYDPEELVGKLVVMVANLAPRKMKFGVSEGMVLAA 650

                         90       100
                 ....*....|....*....|..
gi 113951751 234 SSP-EKVEILDPPSGAAAGDRI 254
Cdd:PRK00133 651 GPGgGDLFLLEPDEGAKPGMRV 672
tRNA_bind_EcMetRS_like cd02800
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ...
 154-254 2.87e-27

tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like proteins. This family includes EcMetRS and Aquifex aeolicus Trbp111 (AaTrbp111). This domain has general tRNA binding properties. MetRS aminoacylates methionine transfer RNAs (tRNAmet). AaTrbp111 is structure-specific molecular chaperone recognizing the L-shape of the tRNA fold. AaTrbp111 plays a role in nuclear trafficking of tRNAs. The functional unit of EcMetRs and AaTrbp111 is a homodimer, this domain acts as the dimerization domain.


Pssm-ID: 239199 [Multi-domain]  Cd Length: 105  Bit Score: 102.58  E-value: 2.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 154 DVSRLDLRVGRIISAEKHPDADSLYVEQVDVGEAaPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCA 233
Cdd:cd02800    5 DFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGEE-ERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAA 83

                         90       100
                 ....*....|....*....|.
gi 113951751 234 SSPEKVEILDPPSGAAAGDRI 254
Cdd:cd02800   84 EDGGKLKLLTPDEEVEPGSRV 104
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 154-254 4.85e-26

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 107.96  E-value: 4.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 154 DVSRLDLRVGRIISAEKHPDADSLYVEQVDVGEAAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCA 233
Cdd:PRK12267 547 DFDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVSGIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAA 626

                         90       100
                 ....*....|....*....|.
gi 113951751 234 SSPEKVEILDPPSGAAAGDRI 254
Cdd:PRK12267 627 EDDGKLTLLTVDKEVPNGSKV 647
tRNA_bind_CsaA cd02798
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ...
 154-254 2.38e-24

tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export related activities. CsaA has a putative tRNA binding activity. The functional unit of CsaA is a homodimer and this domain acts as a dimerization domain.


Pssm-ID: 239197 [Multi-domain]  Cd Length: 107  Bit Score: 95.00  E-value: 2.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 154 DVSRLDLRVGRIISAEKHPDA-DSLYVEQVDVGEAAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMC 232
Cdd:cd02798    5 DFEKVDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLG 84

                         90       100
                 ....*....|....*....|...
gi 113951751 233 ASSP-EKVEILDPPSGAAAGDRI 254
Cdd:cd02798   85 ADDEgGEVVLLVPDREVPNGAKV 107
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
154-252 1.23e-20

tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 92.22  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 154 DVSRLD-LRVGRIISAEKHPDADSLYVEQVDVGEaAPRTVVSGLVKH----IPLDQMQNRMAVLLCNLKPAKMRGVLSQA 228
Cdd:COG0073   37 KVGGLDgLRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGAPNVyagdKVPEALVGAQVPGVVNLKPRKIRGVESEG 115

                         90       100
                 ....*....|....*....|....*...
gi 113951751 229 MVMCASSPEKVE----ILDPPSGAAAGD 252
Cdd:COG0073  116 MLCSAEELGLGEdhdgILELPEDAPPGD 143
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 154-254 2.04e-19

methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) is a class I amino acyl-tRNA ligase. This model describes a region of the methionyl-tRNA synthetase that is present at the C-terminus of MetG in some species (E. coli, B. subtilis, Thermotoga maritima, Methanobacterium thermoautotrophicum), and as a separate beta chain in Aquifex aeolicus. It is absent in a number of other species (e.g. Mycoplasma genitalium, Mycobacterium tuberculosis), while Pyrococcus horikoshii has both a full length MetG and a second protein homologous to the beta chain only. Proteins hit by this model should be called methionyl-tRNA synthetase beta chain if and only if the model metG hits a separate protein not also hit by this model. [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273059 [Multi-domain]  Cd Length: 137  Bit Score: 82.86  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751  154 DVSRLDLRVGRIISAEKHPDADSLYVEQVDVGEAApRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVMCA 233
Cdd:TIGR00399  36 DFEKVDLRVGKILKAERVEKSDKLLKLKLDLGDEK-RQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAA 114

                          90       100
                  ....*....|....*....|..
gi 113951751  234 SSPEKV-EILDPPSGAAAGDRI 254
Cdd:TIGR00399 115 EDDGKVlFLLSPDQEAIAGERI 136
PRK10089 PRK10089
chaperone CsaA;
154-254 3.97e-15

chaperone CsaA;


Pssm-ID: 182232 [Multi-domain]  Cd Length: 112  Bit Score: 70.24  E-value: 3.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 154 DVSRLDLRVGRIISAEKHPDADSL-YVEQVDVG-EAAPRTVVSGLVKHIPLDQMQNRMAVLLCNLKPAKMRGVLSQAMVM 231
Cdd:PRK10089   8 DFEKVDIRVGTIVEAEPFPEARKPaYKLWIDFGeEIGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVL 87

                         90       100
                 ....*....|....*....|....
gi 113951751 232 CASSPE-KVEILDPPSGAAAGDRI 254
Cdd:PRK10089  88 GFEDEDgEVVLLTPDRPVPNGVKL 111
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 160-254 1.29e-10

tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. PheRS aminoacylate phenylalanine transfer RNAs (tRNAphe). PheRSs belong structurally to class II aminoacyl tRNA synthetases (aaRSs) but, as they aminoacylate the 2'OH of the terminal ribose of tRNA they belong functionally to class 1 aaRSs. This domain has general tRNA binding properties and is believed to direct tRNAphe to the active site of the enzyme.


Pssm-ID: 239196 [Multi-domain]  Cd Length: 103  Bit Score: 57.52  E-value: 1.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 160 LRVGRIISAEKHPDADSLYVEQVDVGEAAPRTVVSGlVKHIPLDQMqnrmaVLLCN----------LKPAKMRGVLSQAM 229
Cdd:cd02796    1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCG-APNVRAGDK-----VVVALpgavlpgglkIKKRKLRGVESEGM 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 113951751 230 vMCASS----PEKVE-ILDPPSGAAAGDRI 254
Cdd:cd02796   75 -LCSAKelglGEDSDgIIELPEDAPVGTDI 103
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 162-235 1.12e-09

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 59.41  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113951751 162 VGRIISAEKHPDADSLYVEQVDVGEaAPRTVVSG-------------LVKhipldqmqnrmAVLLCNL--KPAKMRGVLS 226
Cdd:PRK00629  47 VGKVLECEKHPNADKLRVCQVDVGE-EPLQIVCGapnvragdkvpvaLPG-----------AVLPGGFkiKKAKLRGVES 114


                 ....*....
gi 113951751 227 QAMvMCASS 235
Cdd:PRK00629 115 EGM-LCSAS 122
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 5-81 1.32e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 38.52  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 113951751   5 RSLFKMSGHTPSLMRLEqkaAEAEQIIEYLKQQVQLLKEKAIVQATLKEEKKLMVENAKLKKDIEELKKQLLDKEKM 81
Cdd:PRK08476  45 NDLEKVKTNSSDVSEIE---HEIETILKNAREEANKIRQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQLANQKQE 118
Ax_dynein_light pfam10211
Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in ...
 20-75 2.27e-03

Axonemal dynein light chain; Axonemal dynein light chain proteins play a dynamic role in flagellar and cilia motility. Eukaryotic cilia and flagella are complex organelles consisting of a core structure, the axoneme, which is composed of nine microtubule doublets forming a cylinder that surrounds a pair of central singlet microtubules. This ultra-structural arrangement seems to be one of the most stable micro-tubular assemblies known and is responsible for the flagellar and ciliary movement of a large number of organizms ranging from protozoan to mammals. This light chain interacts directly with the N-terminal half of the heavy chains.


Pssm-ID: 463000 [Multi-domain]  Cd Length: 187  Bit Score: 38.32  E-value: 2.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113951751   20 LEQKAAEAEQIIEYLKQQVQLLK------EKAIVQATLKEEKKLMVENAKLKKDIEELKKQL 75
Cdd:pfam10211 124 LEKKIADLEEEKEELEKQVAELKakceaiEKREEERRQAEEKKHAEEIAFLKKTNQQLKAQL 185
PRK13169 PRK13169
DNA replication initiation control protein YabA;
16-80 6.94e-03

DNA replication initiation control protein YabA;


Pssm-ID: 183876  Cd Length: 110  Bit Score: 35.60  E-value: 6.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113951751  16 SLMRLEQkaaeaeQIIEYLKQQVQLlkeKAIVQATLKEEKKLMVENAKLKKDIEELKKQLLDKEK 80
Cdd:PRK13169   9 ALDDLEQ------NLGVLLKELGAL---KKQLAELLEENTALRLENDKLRERLEELEAEEPAKEK 64
 
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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