NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|215490009|ref|NP_001135887|]
View 

aminoacyl tRNA synthase complex-interacting multifunctional protein 1 precursor [Homo sapiens]

Protein Classification

tRNA binding domain-containing protein( domain architecture ID 1001905)

tRNA binding domain-containing protein similar to methionine--tRNA ligase that aminoacylates the 2'-OH of the nucleotide at the 3' of tRNA(Met); it is required for elongation of protein synthesis as well as for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation

CATH:  2.40.50.140
EC:  6.1.1.-
Gene Ontology:  GO:0000049

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02610 super family cl33529
probable methionyl-tRNA synthetase
 140-312 1.61e-85

probable methionyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02610:

Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 273.19  E-value: 1.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 140 SIAGSADSKPIDVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMR 219
Cdd:PLN02610 628 GKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMR 707

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 220 GVLSQAMVMCASSPE--KIEILAPPNGSVPGDRITFDAFPGEPDKELNPKKKIWEQIQPDLHTNDECVATYKGVPFEVKG 297
Cdd:PLN02610 708 GIKSQAMVLAASNSDhtKVELVEPPESAAVGERVTFPGFEGEPDDVLNPKKKVWETLQPDLHTNSELVACYKDVPFTTSA 787

                        170
                 ....*....|....*
gi 215490009 298 kGVCRAQTMSNSGIK 312
Cdd:PLN02610 788 -GVCKVASIANGSIR 801
PRK05431 super family cl35319
seryl-tRNA synthetase; Provisional
 3-79 6.42e-05

seryl-tRNA synthetase; Provisional


The actual alignment was detected with superfamily member PRK05431:

Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.29  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009   3 NNDAVLKRLEQKGAEA--DQIIEYLKQQVSLLKE------------KAILQATLREEK--KLRVENAKLKKEIEELKQEL 66
Cdd:PRK05431  10 NPEAVKEALAKRGFPLdvDELLELDEERRELQTEleelqaernalsKEIGQAKRKGEDaeALIAEVKELKEEIKALEAEL 89

                         90
                 ....*....|....*
gi 215490009  67 --IQAEIQNGVKQIP 79
Cdd:PRK05431  90 deLEAELEELLLRIP 104
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 140-312 1.61e-85

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 273.19  E-value: 1.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 140 SIAGSADSKPIDVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMR 219
Cdd:PLN02610 628 GKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMR 707

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 220 GVLSQAMVMCASSPE--KIEILAPPNGSVPGDRITFDAFPGEPDKELNPKKKIWEQIQPDLHTNDECVATYKGVPFEVKG 297
Cdd:PLN02610 708 GIKSQAMVLAASNSDhtKVELVEPPESAAVGERVTFPGFEGEPDDVLNPKKKVWETLQPDLHTNSELVACYKDVPFTTSA 787

                        170
                 ....*....|....*
gi 215490009 298 kGVCRAQTMSNSGIK 312
Cdd:PLN02610 788 -GVCKVASIANGSIR 801
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 150-252 5.15e-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: 194.75  E-value: 5.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 150 IDVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMC 229
Cdd:cd02799    1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                         90       100
                 ....*....|....*....|....*
gi 215490009 230 ASSP--EKIEILAPPNGSVPGDRIT 252
Cdd:cd02799   81 ASNAdhEKVELLEPPEGAKPGERVT 105
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 157-250 1.07e-35

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: 124.28  E-value: 1.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009  157 LRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCAS--SPE 234
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEelDGG 80

                          90
                  ....*....|....*.
gi 215490009  235 KIEILAPPNGSVPGDR 250
Cdd:pfam01588  81 SVGLLEPPADVPPGTK 96
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
151-249 7.03e-19

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 87.22  E-value: 7.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 151 DVSRLD-LRIGCIITARKHPDADSLYVEEVDVGEiAPRTVVSGLVNH-----VPlEQMQNRMVILLCNLKPAKMRGVLSQ 224
Cdd:COG0073   37 KVGGLDgLRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGAPNVyagdkVP-EALVGAQVPGVVNLKPRKIRGVESE 114

                         90       100
                 ....*....|....*....|....*....
gi 215490009 225 AMVMCASSPEKIE----ILAPPNGSVPGD 249
Cdd:COG0073  115 GMLCSAEELGLGEdhdgILELPEDAPPGD 143
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 151-251 2.74e-17

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: 76.70  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009  151 DVSRLDLRIGCIITARKHPDADSLYVEEVDVGEiAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCA 230
Cdd:TIGR00399  36 DFEKVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAA 114

                          90       100
                  ....*....|....*....|..
gi 215490009  231 -SSPEKIEILAPPNGSVPGDRI 251
Cdd:TIGR00399 115 eDDGKVLFLLSPDQEAIAGERI 136
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 3-79 6.42e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.29  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009   3 NNDAVLKRLEQKGAEA--DQIIEYLKQQVSLLKE------------KAILQATLREEK--KLRVENAKLKKEIEELKQEL 66
Cdd:PRK05431  10 NPEAVKEALAKRGFPLdvDELLELDEERRELQTEleelqaernalsKEIGQAKRKGEDaeALIAEVKELKEEIKALEAEL 89

                         90
                 ....*....|....*
gi 215490009  67 --IQAEIQNGVKQIP 79
Cdd:PRK05431  90 deLEAELEELLLRIP 104
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 22-70 1.84e-03

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 36.34  E-value: 1.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 215490009   22 IEYLKQQVSLLKEKAIlQATLREEKKLRVENAKLKKEIEELKQELIQAE 70
Cdd:pfam07989  21 IHFLEERLEKLAPEQI-EEALKENIELKVELETLQRELKKLKKLLREAE 68
 
Name Accession Description Interval E-value
PLN02610 PLN02610
probable methionyl-tRNA synthetase
 140-312 1.61e-85

probable methionyl-tRNA synthetase


Pssm-ID: 215329 [Multi-domain]  Cd Length: 801  Bit Score: 273.19  E-value: 1.61e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 140 SIAGSADSKPIDVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMR 219
Cdd:PLN02610 628 GKSKAAAEREIDVSRLDIRVGLIVKAEKHPDADSLYVEEIDVGEGAPRTVVSGLVKYIPLEEMQNRKVCVLCNLKPAAMR 707

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 220 GVLSQAMVMCASSPE--KIEILAPPNGSVPGDRITFDAFPGEPDKELNPKKKIWEQIQPDLHTNDECVATYKGVPFEVKG 297
Cdd:PLN02610 708 GIKSQAMVLAASNSDhtKVELVEPPESAAVGERVTFPGFEGEPDDVLNPKKKVWETLQPDLHTNSELVACYKDVPFTTSA 787

                        170
                 ....*....|....*
gi 215490009 298 kGVCRAQTMSNSGIK 312
Cdd:PLN02610 788 -GVCKVASIANGSIR 801
tRNA_bind_EMAP-II_like cd02799
tRNA-binding-domain-containing EMAP2-like proteins. This family contains a diverse fraction of ...
 150-252 5.15e-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: 194.75  E-value: 5.15e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 150 IDVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMC 229
Cdd:cd02799    1 VDPSRLDIRVGKILKVRKHPDADSLYVEEIDLGEEEPRTIVSGLVKFVPLEQMQNRLVVVLCNLKPRKMRGVKSQGMVLC 80

                         90       100
                 ....*....|....*....|....*
gi 215490009 230 ASSP--EKIEILAPPNGSVPGDRIT 252
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 ...
 157-251 7.35e-38

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: 129.95  E-value: 7.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 157 LRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCAS----S 232
Cdd:cd02153    1 LRVGKIVEAEPHPNADKLYVLKVDIGEEKPRQIVSGAANVYPPEELVGKKVVVAVNLKPKKLRGVESEGMLLSAEelglE 80

                         90
                 ....*....|....*....
gi 215490009 233 PEKIEILAPPNGSVPGDRI 251
Cdd:cd02153   81 EGSVGILELPEDAPVGDRI 99
tRNA_bind pfam01588
Putative tRNA binding domain; This domain is found in prokaryotic methionyl-tRNA synthetases, ...
 157-250 1.07e-35

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: 124.28  E-value: 1.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009  157 LRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCAS--SPE 234
Cdd:pfam01588   1 LRVGKVVEAERHPNADKLLVCKVDVGEEEPRQIVSGAVNVYPPEELVGRLVVVVANLKPAKLRGVESEGMILSAEelDGG 80

                          90
                  ....*....|....*.
gi 215490009  235 KIEILAPPNGSVPGDR 250
Cdd:pfam01588  81 SVGLLEPPADVPPGTK 96
metG PRK00133
methionyl-tRNA synthetase; Reviewed
 151-251 4.09e-26

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 108.32  E-value: 4.09e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 151 DVSRLDLRIGCIITARKHPDADSLYVEEVDVGEiAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCA 230
Cdd:PRK00133 572 DFAKVDLRVAKIVEAEKVEGADKLLKLTLDLGE-ETRQVFSGIKSAYDPEELVGKLVVMVANLAPRKMKFGVSEGMVLAA 650

                         90       100
                 ....*....|....*....|..
gi 215490009 231 SSP-EKIEILAPPNGSVPGDRI 251
Cdd:PRK00133 651 GPGgGDLFLLEPDEGAKPGMRV 672
tRNA_bind_EcMetRS_like cd02800
tRNA-binding-domain-containing Escherichia coli methionyl-tRNA synthetase (EcMetRS)-like ...
 151-251 1.50e-24

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: 95.26  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 151 DVSRLDLRIGCIITARKHPDADSLYVEEVDVGEiAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCA 230
Cdd:cd02800    5 DFAKVDLRVGKVLEAERVEGSDKLLKLTVDLGE-EERQIVSGIAKFYPPEELVGKKVVVVANLKPRKLRGVESQGMILAA 83

                         90       100
                 ....*....|....*....|.
gi 215490009 231 SSPEKIEILAPPNGSVPGDRI 251
Cdd:cd02800   84 EDGGKLKLLTPDEEVEPGSRV 104
tRNA_bind_CsaA cd02798
tRNA-binding-domain-containing CsaA-like proteins. CsaA is a molecular chaperone with export ...
 151-251 3.97e-23

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: 91.53  E-value: 3.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 151 DVSRLDLRIGCIITARKHPDA-DSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMC 229
Cdd:cd02798    5 DFEKVDLRVGTIVEVEDFPEArKPAYKLKVDFGEIGVKQSSAQITKYYKPEELIGRQVVAVVNFPPKQIAGVLSEVLVLG 84

                         90       100
                 ....*....|....*....|...
gi 215490009 230 ASSP-EKIEILAPPNGSVPGDRI 251
Cdd:cd02798   85 ADDEgGEVVLLVPDREVPNGAKV 107
PRK12267 PRK12267
methionyl-tRNA synthetase; Reviewed
 151-251 1.14e-22

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237028 [Multi-domain]  Cd Length: 648  Bit Score: 98.33  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 151 DVSRLDLRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCA 230
Cdd:PRK12267 547 DFDKVELRVAEVLEAEKVEKSDKLLKLQVDLGEEEPRQIVSGIAKFYPPEELVGKKVVVVANLKPAKLMGEESQGMILAA 626

                         90       100
                 ....*....|....*....|.
gi 215490009 231 SSPEKIEILAPPNGSVPGDRI 251
Cdd:PRK12267 627 EDDGKLTLLTVDKEVPNGSKV 647
EMAP COG0073
tRNA-binding EMAP/Myf domain [Translation, ribosomal structure and biogenesis];
151-249 7.03e-19

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


Pssm-ID: 439843 [Multi-domain]  Cd Length: 773  Bit Score: 87.22  E-value: 7.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 151 DVSRLD-LRIGCIITARKHPDADSLYVEEVDVGEiAPRTVVSGLVNH-----VPlEQMQNRMVILLCNLKPAKMRGVLSQ 224
Cdd:COG0073   37 KVGGLDgLRVGKVLEAEPHPNADKLLVLQVDVGE-ETRQIVCGAPNVyagdkVP-EALVGAQVPGVVNLKPRKIRGVESE 114

                         90       100
                 ....*....|....*....|....*....
gi 215490009 225 AMVMCASSPEKIE----ILAPPNGSVPGD 249
Cdd:COG0073  115 GMLCSAEELGLGEdhdgILELPEDAPPGD 143
metG_C_term TIGR00399
methionyl-tRNA synthetase C-terminal region/beta chain; The methionyl-tRNA synthetase (metG) ...
 151-251 2.74e-17

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: 76.70  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009  151 DVSRLDLRIGCIITARKHPDADSLYVEEVDVGEiAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVMCA 230
Cdd:TIGR00399  36 DFEKVDLRVGKILKAERVEKSDKLLKLKLDLGD-EKRQIVSGIAGYYTPEELVGKKVIVVANLKPAKLFGVKSEGMILAA 114

                          90       100
                  ....*....|....*....|..
gi 215490009  231 -SSPEKIEILAPPNGSVPGDRI 251
Cdd:TIGR00399 115 eDDGKVLFLLSPDQEAIAGERI 136
PRK10089 PRK10089
chaperone CsaA;
151-251 4.92e-16

chaperone CsaA;


Pssm-ID: 182232 [Multi-domain]  Cd Length: 112  Bit Score: 72.56  E-value: 4.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 151 DVSRLDLRIGCIITARKHPDADSL-YVEEVDVG-EIAPRTVVSGLVNHVPLEQMQNRMVILLCNLKPAKMRGVLSQAMVM 228
Cdd:PRK10089   8 DFEKVDIRVGTIVEAEPFPEARKPaYKLWIDFGeEIGVKQSSAQITPHYTPEELIGKQVVAVVNFPPKQIAGFMSEVLVL 87

                         90       100
                 ....*....|....*....|....
gi 215490009 229 CASSPEKIEILAPPNGSVP-GDRI 251
Cdd:PRK10089  88 GFEDEDGEVVLLTPDRPVPnGVKL 111
tRNA_bind_bactPheRS cd02796
tRNA-binding-domain-containing prokaryotic phenylalanly tRNA synthetase (PheRS) beta chain. ...
 157-230 1.14e-08

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: 52.13  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 157 LRIGCIITARKHPDADSLYVEEVDVGEIAPRTVVSGLVNHVpleqmQNRMVIL---------LCNLKPAKMRGVLSQAMv 227
Cdd:cd02796    1 VVVGKVLEVEPHPNADKLNVCKVDIGENKPLQIVCGAPNVR-----AGDKVVValpgavlpgGLKIKKRKLRGVESEGM- 74


                 ...
gi 215490009 228 MCA 230
Cdd:cd02796   75 LCS 77
pheT PRK00629
phenylalanyl-tRNA synthetase subunit beta; Reviewed
 159-232 2.73e-07

phenylalanyl-tRNA synthetase subunit beta; Reviewed


Pssm-ID: 234804 [Multi-domain]  Cd Length: 791  Bit Score: 51.71  E-value: 2.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009 159 IGCIITARKHPDADSLYVEEVDVGEiAPRTVVSGLVN-----HVPL----EQMQNRMVIllcnlKPAKMRGVLSQAMvMC 229
Cdd:PRK00629  47 VGKVLECEKHPNADKLRVCQVDVGE-EPLQIVCGAPNvragdKVPValpgAVLPGGFKI-----KKAKLRGVESEGM-LC 119


                 ...
gi 215490009 230 ASS 232
Cdd:PRK00629 120 SAS 122
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 3-79 6.42e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 44.29  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215490009   3 NNDAVLKRLEQKGAEA--DQIIEYLKQQVSLLKE------------KAILQATLREEK--KLRVENAKLKKEIEELKQEL 66
Cdd:PRK05431  10 NPEAVKEALAKRGFPLdvDELLELDEERRELQTEleelqaernalsKEIGQAKRKGEDaeALIAEVKELKEEIKALEAEL 89

                         90
                 ....*....|....*
gi 215490009  67 --IQAEIQNGVKQIP 79
Cdd:PRK05431  90 deLEAELEELLLRIP 104
PRK08476 PRK08476
F0F1 ATP synthase subunit B'; Validated
 1-66 1.52e-03

F0F1 ATP synthase subunit B'; Validated


Pssm-ID: 181442 [Multi-domain]  Cd Length: 141  Bit Score: 38.13  E-value: 1.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215490009   1 MANNDAVLKRLEQK-----------GAEADQIIEYLKQQVSLLKEKAILQATLREEKKLRVENAKLKKEIEELKQEL 66
Cdd:PRK08476  36 MDNRNASIKNDLEKvktnssdvseiEHEIETILKNAREEANKIRQKAIAKAKEEAEKKIEAKKAELESKYEAFAKQL 112
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 22-70 1.84e-03

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 36.34  E-value: 1.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 215490009   22 IEYLKQQVSLLKEKAIlQATLREEKKLRVENAKLKKEIEELKQELIQAE 70
Cdd:pfam07989  21 IHFLEERLEKLAPEQI-EEALKENIELKVELETLQRELKKLKKLLREAE 68
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 3-66 2.80e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.42  E-value: 2.80e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215490009    3 NNDAVLKRLEQKGAEADQIIEYLKQQVSllkekailqatlREEKKLRVENAKLKKEIEELKQEL 66
Cdd:pfam10174 433 NTDTALTTLEEALSEKERIIERLKEQRE------------REDRERLEELESLKKENKDLKEKV 484
PRK13169 PRK13169
DNA replication initiation control protein YabA;
20-65 9.08e-03

DNA replication initiation control protein YabA;


Pssm-ID: 183876  Cd Length: 110  Bit Score: 35.22  E-value: 9.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 215490009  20 QIIEYLKQQVSLLKEKaiLQATLREEKKLRVENAKLKKEIEELKQE 65
Cdd:PRK13169  15 QNLGVLLKELGALKKQ--LAELLEENTALRLENDKLRERLEELEAE 58
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 7-68 9.46e-03

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 34.16  E-value: 9.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215490009    7 VLKRLEQKGAEADQIIEYLKQQVSLLKEKAilqATLREEKK-LRVENAKLKKEIEELKQELIQ 68
Cdd:pfam06005   5 LLEQLETKIQAAVDTIALLQMENEELKEEN---EELKEEANeLEEENQQLKQERNQWQERIRG 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH