NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907191153|ref|XP_036010192|]
View 

probable cysteine--tRNA ligase, mitochondrial isoform X7 [Mus musculus]

Protein Classification

cysteine--tRNA ligase( domain architecture ID 1002819)

cysteine--tRNA ligase catalyzes the attachment of cysteine to tRNA(Cys)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PTZ00399 super family cl36555
cysteinyl-tRNA-synthetase; Provisional
8-430 8.11e-138

cysteinyl-tRNA-synthetase; Provisional


The actual alignment was detected with superfamily member PTZ00399:

Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 409.42  E-value: 8.11e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDLHA-RGDK--YGKLVNTVPSAT 84
Cdd:PTZ00399  128 LARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVEAfRKAGhvYPKLEPESVADE 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  85 AEPGD---------SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENE 155
Cdd:PTZ00399  207 DRIAEgegalgkvsGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNE 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 156 IAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHL 235
Cdd:PTZ00399  287 LAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEK 364
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 236 LLGLASFVEDARAYVKGQLTCGPVEEDV----LWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKeas 311
Cdd:PTZ00399  365 DKVFFNFFANVKIKLRESELTSPQKWTQhdfeLNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGEQ--- 441
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 312 gPRSPTVFgAIISYVEQFFETVGISLANRQC-VSGDSSTV-TLRCVVDELVRFRLKVRQYAldtpgAAGEARKRQLQERQ 389
Cdd:PTZ00399  442 -PSAPLLR-SVAQYVTKILSIFGLVEGSDGLgSQGQNSTSeNFKPLLEALLRFRDEVRDAA-----KAEMKLISLDKKKK 514
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1907191153 390 PLLEACDTLR-QDLVTHGINVKDRGSAASTWELLDP----RTRHQK 430
Cdd:PTZ00399  515 QLLQLCDKLRdEWLPNLGIRIEDKPDGPSVWKLDDKeelqREKEEK 560
 
Name Accession Description Interval E-value
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
8-430 8.11e-138

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 409.42  E-value: 8.11e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDLHA-RGDK--YGKLVNTVPSAT 84
Cdd:PTZ00399  128 LARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVEAfRKAGhvYPKLEPESVADE 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  85 AEPGD---------SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENE 155
Cdd:PTZ00399  207 DRIAEgegalgkvsGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNE 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 156 IAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHL 235
Cdd:PTZ00399  287 LAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEK 364
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 236 LLGLASFVEDARAYVKGQLTCGPVEEDV----LWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKeas 311
Cdd:PTZ00399  365 DKVFFNFFANVKIKLRESELTSPQKWTQhdfeLNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGEQ--- 441
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 312 gPRSPTVFgAIISYVEQFFETVGISLANRQC-VSGDSSTV-TLRCVVDELVRFRLKVRQYAldtpgAAGEARKRQLQERQ 389
Cdd:PTZ00399  442 -PSAPLLR-SVAQYVTKILSIFGLVEGSDGLgSQGQNSTSeNFKPLLEALLRFRDEVRDAA-----KAEMKLISLDKKKK 514
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1907191153 390 PLLEACDTLR-QDLVTHGINVKDRGSAASTWELLDP----RTRHQK 430
Cdd:PTZ00399  515 QLLQLCDKLRdEWLPNLGIRIEDKPDGPSVWKLDDKeelqREKEEK 560
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
2-421 8.27e-133

Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439985 [Multi-domain]  Cd Length: 465  Bit Score: 390.23  E-value: 8.27e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   2 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVP 81
Cdd:COG0215    82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  82 -----SATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 156
Cdd:COG0215   160 ddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEI 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 157 AQSEVFHqCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLL 236
Cdd:COG0215   239 AQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKAL 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 237 LGLASFVEDARAYVKgqltcgpvEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLravskeaSGPRSP 316
Cdd:COG0215   316 ERLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAL-------DEGEDK 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 317 TVFGAIISYVEQFFETVGISLANRQCVSGDSSTVtlrcVVDELVRFRLKVRQyaldtpgaagEARKRQLQERqplleAcD 396
Cdd:COG0215   381 AALAALAALLRALGGVLGLLLLEPEAWQGAAEDE----LLDALIEALIEERA----------EARKAKDFAR-----A-D 440
                         410       420
                  ....*....|....*....|....*
gi 1907191153 397 TLRQDLVTHGINVKDrGSAASTWEL 421
Cdd:COG0215   441 RIRDELAALGIVLED-TPDGTTWRR 464
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
8-233 2.55e-103

tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 308.91  E-value: 2.55e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKL----VNTVPSA 83
Cdd:pfam01406  75 LAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLsgqnLEQLEAG 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  84 TAEPGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFH 163
Cdd:pfam01406 154 ARGEVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAF 233
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 164 QcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 233
Cdd:pfam01406 234 D-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
cysS TIGR00435
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ...
2-300 4.66e-102

cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273076 [Multi-domain]  Cd Length: 464  Bit Score: 311.62  E-value: 4.66e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   2 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVNTVP 81
Cdd:TIGR00435  81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKQDL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  82 S-----ATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 156
Cdd:TIGR00435 160 DqleagARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEI 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 157 AQSEVFHQcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK--- 233
Cdd:TIGR00435 239 AQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKnal 315
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191153 234 -HLLLGLASFVEDArAYVKGQ-LTCGPVEEDVlwerltstKKAVKAALANDFDTPRAVNTILDLVHHAN 300
Cdd:TIGR00435 316 eRLYKALRVLDTSL-AYSGNQsLNKFPDEKEF--------EARFVEAMDDDLNTANALAVLFELAKSIN 375
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
1-225 1.22e-61

catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173899 [Multi-domain]  Cd Length: 213  Bit Score: 198.96  E-value: 1.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   1 MNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntv 80
Cdd:cd00672    79 EGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------------------------- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  81 psataepgdsdkrhssdfalwkaakpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSE 160
Cdd:cd00672   113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907191153 161 VFHQCqQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 225
Cdd:cd00672   152 AATGK-PFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
 
Name Accession Description Interval E-value
PTZ00399 PTZ00399
cysteinyl-tRNA-synthetase; Provisional
8-430 8.11e-138

cysteinyl-tRNA-synthetase; Provisional


Pssm-ID: 240402 [Multi-domain]  Cd Length: 651  Bit Score: 409.42  E-value: 8.11e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYStATGSVYFDLHA-RGDK--YGKLVNTVPSAT 84
Cdd:PTZ00399  128 LARKWEKEFFEDMKALNVRPPDVITRVSEYVPEIVDFIQKIIDNGFAYE-SNGSVYFDVEAfRKAGhvYPKLEPESVADE 206
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  85 AEPGD---------SDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENE 155
Cdd:PTZ00399  207 DRIAEgegalgkvsGEKRSPNDFALWKASKPGEPSWDSPWGKGRPGWHIECSAMASNILGDPIDIHSGGIDLKFPHHDNE 286
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 156 IAQSEVFHQCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHL 235
Cdd:PTZ00399  287 LAQSEAYFDKHQWVNYFLHSGHLHIKG--LKMSKSLKNFITIRQALSKYTARQIRLLFLLHKWDKPMNYSDESMDEAIEK 364
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 236 LLGLASFVEDARAYVKGQLTCGPVEEDV----LWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKeas 311
Cdd:PTZ00399  365 DKVFFNFFANVKIKLRESELTSPQKWTQhdfeLNELFEETKSAVHAALLDNFDTPEALQALQKLISATNTYLNSGEQ--- 441
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 312 gPRSPTVFgAIISYVEQFFETVGISLANRQC-VSGDSSTV-TLRCVVDELVRFRLKVRQYAldtpgAAGEARKRQLQERQ 389
Cdd:PTZ00399  442 -PSAPLLR-SVAQYVTKILSIFGLVEGSDGLgSQGQNSTSeNFKPLLEALLRFRDEVRDAA-----KAEMKLISLDKKKK 514
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1907191153 390 PLLEACDTLR-QDLVTHGINVKDRGSAASTWELLDP----RTRHQK 430
Cdd:PTZ00399  515 QLLQLCDKLRdEWLPNLGIRIEDKPDGPSVWKLDDKeelqREKEEK 560
CysS COG0215
Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA ...
2-421 8.27e-133

Cysteinyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Cysteinyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439985 [Multi-domain]  Cd Length: 465  Bit Score: 390.23  E-value: 8.27e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   2 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKLVNTVP 81
Cdd:COG0215    82 GESIWELAERYIAAFHEDMDALGVLPPDIEPRATEHIPEMIELIERLIEKGHAY-EADGDVYFDV-RSFPDYGKLSGRNL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  82 -----SATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 156
Cdd:COG0215   160 ddlraGARVEV-DEEKRDPLDFALWKAAKPGEPSWDSPWGRGRPGWHIECSAMSTKYLGETFDIHGGGIDLIFPHHENEI 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 157 AQSEVFHqCQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLL 236
Cdd:COG0215   239 AQSEAAT-GKPFARYWMHNGFLTVNG--EKMSKSLGNFFTVRDLLKKYDPEVLRFFLLSAHYRSPLDFSEEALEEAEKAL 315
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 237 LGLASFVEDARAYVKgqltcgpvEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANRQLravskeaSGPRSP 316
Cdd:COG0215   316 ERLYNALRRLEEALG--------AADSSAEEIEELREEFIAAMDDDFNTPEALAVLFELVREINKAL-------DEGEDK 380
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 317 TVFGAIISYVEQFFETVGISLANRQCVSGDSSTVtlrcVVDELVRFRLKVRQyaldtpgaagEARKRQLQERqplleAcD 396
Cdd:COG0215   381 AALAALAALLRALGGVLGLLLLEPEAWQGAAEDE----LLDALIEALIEERA----------EARKAKDFAR-----A-D 440
                         410       420
                  ....*....|....*....|....*
gi 1907191153 397 TLRQDLVTHGINVKDrGSAASTWEL 421
Cdd:COG0215   441 RIRDELAALGIVLED-TPDGTTWRR 464
tRNA-synt_1e pfam01406
tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA ...
8-233 2.55e-103

tRNA synthetases class I (C) catalytic domain; This family includes only cysteinyl tRNA synthetases.


Pssm-ID: 396128 [Multi-domain]  Cd Length: 301  Bit Score: 308.91  E-value: 2.55e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHArGDKYGKL----VNTVPSA 83
Cdd:pfam01406  75 LAARFIEAYTKDMDALNVLPPDLEPRVTEHIDEIIEFIERLIKKGYAYVSDNGDVYFDVSS-FPDYGKLsgqnLEQLEAG 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  84 TAEPGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFH 163
Cdd:pfam01406 154 ARGEVSEGKRDPLDFALWKASKEGEPSWDSPWGKGRPGWHIECSAMARKYLGDQIDIHGGGIDLAFPHHENEIAQSEAAF 233
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 164 QcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK 233
Cdd:pfam01406 234 D-KQLANYWLHNGHVMIDG--EKMSKSLGNFFTIRDVLKRYDPEILRYFLLSVHYRSPLDFSEELLEQAK 300
cysS TIGR00435
cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not ...
2-300 4.66e-102

cysteinyl-tRNA synthetase; This model finds the cysteinyl-tRNA synthetase from most but not from all species. The enzyme from one archaeal species, Archaeoglobus fulgidus, is found but the equivalent enzymes from some other Archaea, including Methanococcus jannaschii, are not found, although biochemical evidence suggests that tRNA(Cys) in these species are charged directly with Cys rather than through a misacylation and correction pathway as for tRNA(Gln). [Protein synthesis, tRNA aminoacylation]


Pssm-ID: 273076 [Multi-domain]  Cd Length: 464  Bit Score: 311.62  E-value: 4.66e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   2 NVTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYFDLHARgDKYGKLVNTVP 81
Cdd:TIGR00435  81 GESVYEVSERFIEAYFEDMKALNVLPPDLEPRATEHIDEIIEFIEQLIEKGYAYVSDNGDVYFDVSKF-KDYGKLSKQDL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  82 S-----ATAEPgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEI 156
Cdd:TIGR00435 160 DqleagARVDV-DEAKRNKLDFVLWKSSKEGEPKWDSPWGKGRPGWHIECSAMNDKYLGDQIDIHGGGVDLIFPHHENEI 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 157 AQSEVFHQcQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK--- 233
Cdd:TIGR00435 239 AQSEAAFG-KQLAKYWMHNGFLMIDN--EKMSKSLGNFFTVRDVLKNYDPEILRYFLLSVHYRSPLDFSEELLEAAKnal 315
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907191153 234 -HLLLGLASFVEDArAYVKGQ-LTCGPVEEDVlwerltstKKAVKAALANDFDTPRAVNTILDLVHHAN 300
Cdd:TIGR00435 316 eRLYKALRVLDTSL-AYSGNQsLNKFPDEKEF--------EARFVEAMDDDLNTANALAVLFELAKSIN 375
PLN02946 PLN02946
cysteine-tRNA ligase
5-232 5.33e-67

cysteine-tRNA ligase


Pssm-ID: 178532 [Multi-domain]  Cd Length: 557  Bit Score: 223.27  E-value: 5.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   5 PASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTAtGSVYFDLHaRGDKYGKLV------N 78
Cdd:PLN02946  143 PISLSRRYCEEFLSDMAYLHCLPPSVEPRVSDHIPQIIDMIKQILDNGCAYRVD-GDVYFSVD-KFPEYGKLSgrkledN 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  79 TVPSATAEpgDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQ 158
Cdd:PLN02946  221 RAGERVAV--DSRKKNPADFALWKAAKEGEPFWDSPWGPGRPGWHIECSAMSAAYLGHSFDIHGGGMDLVFPHHENEIAQ 298
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907191153 159 SEVfHQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEA 232
Cdd:PLN02946  299 SCA-ACCDSNISYWIHNGFVTVD--SEKMSKSLGNFFTIRQVIDLYHPLALRLFLLGTHYRSPINYSDVQLESA 369
cysS PRK14535
cysteinyl-tRNA synthetase; Provisional
4-319 4.14e-66

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173001 [Multi-domain]  Cd Length: 699  Bit Score: 224.21  E-value: 4.14e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   4 TPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYSTATGSVYF---DLHARGDKYGKLVNTV 80
Cdd:PRK14535  310 TIGELTARFIQAMHEDADALGVLRPDIEPKATENIPQMIAMIETLIQNGKAYPAANGDVYYavrEFAAYGQLSGKSLDDL 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  81 PSATAEPGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQS- 159
Cdd:PRK14535  390 RAGERVEVDGFKRDPLDFVLWKAAKAGEPAWESPWGNGRPGWHIECSAMSENLFGDTFDIHGGGADLQFPHHENEIAQSv 469
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 160 -EVFHQCQQWG-------------NYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 225
Cdd:PRK14535  470 gATGHTCGHHHaqthhgqsiashvKYWLHNGFIRVDG--EKMSKSLGNFFTIREVLKQYDPEVVRFFILRAHYRSPLNYS 547
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 226 DSTLVEAKHLLLGLASFVEDArayvkgqltcgPVEEDVLWERLTSTKKAVKAALANDFDTPRAVNTILDLVHHANR---- 301
Cdd:PRK14535  548 DAHLDDAKGALTRLYTTLKNT-----------PAAEFMLSENVNDYTRRFYAAMNDDFGTVEAVAVLFELAGEVNKtnda 616
                         330       340
                  ....*....|....*....|...
gi 1907191153 302 QLRAVSKEASG-----PRSPTVF 319
Cdd:PRK14535  617 QLAGCLKALGGiigllQRDPTEF 639
CysRS_core cd00672
catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) ...
1-225 1.22e-61

catalytic core domain of cysteinyl tRNA synthetase; Cysteinyl tRNA synthetase (CysRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173899 [Multi-domain]  Cd Length: 213  Bit Score: 198.96  E-value: 1.22e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   1 MNVTPASLASLFEEEFKQDMAALKVLPPTVYLRVtenipqiiafiegiiahghaystatgsvyfdlhargdkygklvntv 80
Cdd:cd00672    79 EGLSWKEVADYYTKEFFEDMKALNVLPPDVVPRV---------------------------------------------- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  81 psataepgdsdkrhssdfalwkaakpqevfwaspwgdgrpgWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSE 160
Cdd:cd00672   113 -----------------------------------------WHIECSAMAMKYLGETFDIHGGGVDLIFPHHENEIAQSE 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907191153 161 VFHQCqQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 225
Cdd:cd00672   152 AATGK-PFARYWLHTGHLTIDG--EKMSKSLGNFITVRDALKKYDPEVLRLALLSSHYRSPLDFS 213
PRK12418 PRK12418
cysteinyl-tRNA synthetase; Provisional
16-292 1.27e-53

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 183518 [Multi-domain]  Cd Length: 384  Bit Score: 183.59  E-value: 1.27e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  16 FKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHARGDkYGKLVNTVPSATAE------ 86
Cdd:PRK12418   83 FREDMEALRVLPPRDYVGAVESIPEVVELVEKLLASGAAYvvdDEEYPDVYFSVDATPQ-FGYESGYDRATMLElfaerg 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  87 --PGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQ 164
Cdd:PRK12418  162 gdPDRPGKRDPLDALLWRAARPGEPSWPSPFGPGRPGWHIECSAIALNRLGSGFDIQGGGSDLIFPHHEFSAAHAEAATG 241
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 165 CQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfv 243
Cdd:PRK12418  242 ERRFARHYVHAGMIGLDG--EKMSKSRGNLVFVSRLRAAgVDPAAIRLALLAGHYRADREWTDAVLAEAEARL------- 312
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1907191153 244 EDARAYVKgqLTCGPVEEDVLwerltstkKAVKAALANDFDTPRAVNTI 292
Cdd:PRK12418  313 ARWRAAAA--LPAGPDAADVV--------ARVRAALADDLDTPGALAAV 351
mycothiol_MshC TIGR03447
cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this ...
16-288 2.70e-51

cysteine--1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase; Members of this protein family are MshC, l-cysteine:1-D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, an enzyme that uses ATP to ligate a Cys residue to a mycothiol precursor molecule, in the second to last step in mycothiol biosynthesis. This enzyme shows considerable homology to Cys--tRNA ligases, and many instances are misannotated as such. Mycothiol is found in Mycobacterium tuberculosis, Corynebacterium glutamicum, Streptomyces coelicolor, and various other members of the Actinobacteria. Mycothiol is an analog to glutathione. [Biosynthesis of cofactors, prosthetic groups, and carriers, Glutathione and analogs]


Pssm-ID: 132488 [Multi-domain]  Cd Length: 411  Bit Score: 177.99  E-value: 2.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  16 FKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAY---STATGSVYFDLHArGDKYGKLVN----TVPSATAE-- 86
Cdd:TIGR03447 110 FREDMEALRVLPPRDYIGAVESIDEVVEMVEKLLASGAAYiveGPEYPDVYFSIDA-TEQFGYESGydraTMLELFAErg 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  87 --PGDSDKRHSSDFALWKAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSEVFHQ 164
Cdd:TIGR03447 189 gdPDRPGKRDPLDALLWRAAREGEPSWDSPFGRGRPGWHIECSAIALNRLGAGFDIQGGGSDLIFPHHEFSAAHAEAATG 268
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 165 CQQWGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKT-FSPDVFRLFCLRTNYRSAIEYSDSTLVEAKHLLlglasfv 243
Cdd:TIGR03447 269 VRRMARHYVHAGMIGLDG--EKMSKSLGNLVFVSKLRAAgVDPAAIRLGLLAGHYRQDRDWTDAVLAEAEARL------- 339
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1907191153 244 edARAYVKGQLTCGPVEEDVLwerltstkKAVKAALANDFDTPRA 288
Cdd:TIGR03447 340 --ARWRAALALPDAPDATDLI--------ARLRQHLANDLDTPAA 374
cysS PRK14536
cysteinyl-tRNA synthetase; Provisional
8-296 8.59e-50

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 184731 [Multi-domain]  Cd Length: 490  Bit Score: 175.88  E-value: 8.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   8 LASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLHARGDkYGKLVNT----VPSA 83
Cdd:PRK14536   99 IAAHYTAAFFRDTARLNIERPSIVCNATEHIQDMIALIKRLEARGHTY-CAGGNVYFDIRTFPS-YGSLASAavedLQAG 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  84 TAEPGDSDKRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHENEIAQSE 160
Cdd:PRK14536  177 ARIEHDTNKRNPHDFVLWftrSKFENHALTWDSPWGRGYPGWHIECSAMSMKYLGEQCDIHIGGVDHIRVHHTNEIAQCE 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 161 VFhQCQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDFL-KTFSPDVFRLFCLRTNYRSAIEYSDSTLVEAK----HL 235
Cdd:PRK14536  257 AA-TGKPWVRYWLHHEFLLMN--KGKMSKSAGQFLTLSSLQeKGFQPLDYRFFLLGGHYRSQLAFSWEALKTAKaarrSL 333
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907191153 236 LLGLASFVEDARAY---VKGQLTcgpveeDVLWERLTSTKKA--------VKAALANDFDTPRAVNTILDLV 296
Cdd:PRK14536  334 VRRVARVVDAARATtgsVRGTLA------ECAAERVAESRASesellltdFRAALEDDFSTPKALSELQKLV 399
cysS PRK14534
cysteinyl-tRNA synthetase; Provisional
3-233 2.59e-40

cysteinyl-tRNA synthetase; Provisional


Pssm-ID: 173000 [Multi-domain]  Cd Length: 481  Bit Score: 150.00  E-value: 2.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153   3 VTPASLASLFEEEFKQDMAALKVLPPTVYLRVTENIPQIIAFIEGIIAHGHAYsTATGSVYFDLhARGDKYGKL----VN 78
Cdd:PRK14534   92 LTVYEISRFFTEAFFDDCKKLNIVYPDKVLVASEYIPIMIEVVKVLEENGFTY-FVNGNVYFDT-SCFKSYGQMaginLN 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153  79 TVPSATAEPGDSD--KRHSSDFALW---KAAKPQEVFWASPWGDGRPGWHIECSTMASEVFGSHLDIHTGGIDLAFPHHE 153
Cdd:PRK14534  170 DFKDMSVSRVEIDksKRNKSDFVLWftnSKFKDQEMKWDSPWGFGYPSWHLECAAMNLEYFKSTLDIHLGGVDHIGVHHI 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 154 NEIAQSEVFHQcQQWGNYFLHSGHLHVKgtEEKMSKSLKNYITIKDF-LKTFSPDVFRLFCLRTNYRSAIEYSDSTLVEA 232
Cdd:PRK14534  250 NEIAIAECYLN-KKWCDMFVHGEFLIME--YEKMSKSNNNFITIKDLeDQGFSPLDFRYFCLTAHYRTQLKFTFNNLKAC 326

                  .
gi 1907191153 233 K 233
Cdd:PRK14534  327 K 327
MetG COG0143
Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA ...
175-301 5.19e-09

Methionyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Methionyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439913 [Multi-domain]  Cd Length: 544  Bit Score: 58.20  E-value: 5.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 175 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSA-IEYSDSTLVE-------AK--HLLLGLASFVE 244
Cdd:COG0143   318 HGFLTVEG--EKMSKSRGNVIDPDDLLDRYGPDALRYYLLREVPFGQdGDFSWEDFVArvnsdlaNDlgNLASRTLSMIH 395
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 245 darAYVKGQLTCGPVEEDV---LWERLTSTKKAVKAALANdFDTPRAVNTILDLVHHANR 301
Cdd:COG0143   396 ---KYFDGKVPEPGELTEAdeeLLAEAEAALEEVAEAMEA-FEFRKALEEIMALARAANK 451
LeuRS_core cd00812
catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic ...
138-212 4.59e-07

catalytic core domain of leucyl-tRNA synthetases; Leucyl tRNA synthetase (LeuRS) catalytic core domain. This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. In Aquifex aeolicus, the gene encoding LeuRS is split in two, just before the KMSKS motif. Consequently, LeuRS is a heterodimer, which likely superimposes with the LeuRS monomer found in most other organisms. LeuRS has an insertion in the core domain, which is subject to both deletions and rearrangements and thus differs between prokaryotic LeuRS and archaeal/eukaryotic LeuRS. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 173906 [Multi-domain]  Cd Length: 314  Bit Score: 51.48  E-value: 4.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 138 LDIHTGGIDLAFPH-----------HENEIAQSEVFHQcqqwgnyFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSP 206
Cdd:cd00812   225 VDIYIGGKEHAPNHllysrfnhkalFDEGLVTDEPPKG-------LIVQGMVLLEG--EKMSKSKGNVVTPDEAIKKYGA 295

                  ....*.
gi 1907191153 207 DVFRLF 212
Cdd:cd00812   296 DAARLY 301
IleS COG0060
Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA ...
186-296 1.67e-06

Isoleucyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Isoleucyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


Pssm-ID: 439830 [Multi-domain]  Cd Length: 931  Bit Score: 50.46  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 186 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYSDSTLVE-AKHL---------LLG-LASFVEDARAYVKGQL 254
Cdd:COG0060   603 KMSKSLGNVVDPQEVIDKYGADILRLWVASSDYWGDLRFSDEILKEvRDVYrrlrntyrfLLAnLDDFDPAEDAVPYEDL 682
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907191153 255 TcgpvEED--VLwERLTSTKKAVKAALaNDFDTPRAVNTILDLV 296
Cdd:COG0060   683 P----ELDrwIL-SRLNELIKEVTEAY-DNYDFHRAYRALHNFC 720
MetRS_core cd00814
catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) ...
175-227 2.19e-06

catalytic core domain of methioninyl-tRNA synthetases; Methionine tRNA synthetase (MetRS) catalytic core domain. This class I enzyme aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. MetRS, which consists of the core domain and an anti-codon binding domain, functions as a monomer. However, in some species the anti-codon binding domain is followed by an EMAP domain. In this case, MetRS functions as a homodimer. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. As a result of a deletion event, MetRS has a significantly shorter core domain insertion than IleRS, ValRS, and LeuR. Consequently, the MetRS insertion lacks the editing function.


Pssm-ID: 173907 [Multi-domain]  Cd Length: 319  Bit Score: 49.07  E-value: 2.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907191153 175 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLrtnyRSAIEYSDS 227
Cdd:cd00814   271 HGYLTVEG--KKMSKSRGNVVDPDDLLERYGADALRYYLL----RERPEGKDS 317
metG PRK00133
methionyl-tRNA synthetase; Reviewed
175-301 5.97e-05

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 234655 [Multi-domain]  Cd Length: 673  Bit Score: 45.53  E-value: 5.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907191153 175 SGHLHVKGteEKMSKSlKNY-ITIKDFLKTFSPDVFRlFCLRTNYRSAIEYSD-----------STLVeAKhllLG-LAS 241
Cdd:PRK00133  320 HGFLTVEG--AKMSKS-RGTfIWARTYLDHLDPDYLR-YYLAAKLPETIDDLDfnwedfqqrvnSELV-GK---VVnFAS 391
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907191153 242 ----FVEDaraYVKGQLTCGPVEEDvLWERLTSTKKAVKAALaNDFDTPRAVNTILDLVHHANR 301
Cdd:PRK00133  392 rtagFINK---RFDGKLPDALADPE-LLEEFEAAAEKIAEAY-EAREFRKALREIMALADFANK 450
tRNA-synt_1g pfam09334
tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.
175-231 1.17e-04

tRNA synthetases class I (M); This family includes methionyl tRNA synthetases.


Pssm-ID: 401322 [Multi-domain]  Cd Length: 387  Bit Score: 44.20  E-value: 1.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907191153 175 SGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLR-TNYRSAIEYSDSTLVE 231
Cdd:pfam09334 315 HGYLTYEG--GKMSKSRGNVVWPSEALDRFPPDALRYYLARnRPETKDTDFSWEDFVE 370
class_I_aaRS_core cd00802
catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA ...
121-191 1.32e-04

catalytic core domain of class I amino acyl-tRNA synthetase; Class I amino acyl-tRNA synthetase (aaRS) catalytic core domain. These enzymes are mostly monomers which aminoacylate the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.


Pssm-ID: 173901 [Multi-domain]  Cd Length: 143  Bit Score: 42.08  E-value: 1.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907191153 121 GWHIECSTMASEVFGSHLDIHTGGIDLAFpHHENEIAQSEVFHqcQQWGNYFLHSGHLHVKGTeEKMSKSL 191
Cdd:cd00802    77 EYMFLQAADFLLLYETECDIHLGGSDQLG-HIELGLELLKKAG--GPARPFGLTFGRVMGADG-TKMSKSK 143
PRK11893 PRK11893
methionyl-tRNA synthetase; Reviewed
171-216 1.56e-04

methionyl-tRNA synthetase; Reviewed


Pssm-ID: 237012 [Multi-domain]  Cd Length: 511  Bit Score: 43.72  E-value: 1.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907191153 171 YFLHsGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRLFCLRT 216
Cdd:PRK11893  287 VFAH-GFLTLDG--EKMSKSLGNVIDPFDLVDEYGVDAVRYFLLRE 329
leuS PRK12300
leucyl-tRNA synthetase; Reviewed
185-212 2.80e-04

leucyl-tRNA synthetase; Reviewed


Pssm-ID: 237049 [Multi-domain]  Cd Length: 897  Bit Score: 43.32  E-value: 2.80e-04
                          10        20
                  ....*....|....*....|....*...
gi 1907191153 185 EKMSKSLKNYITIKDFLKTFSPDVFRLF 212
Cdd:PRK12300  576 KKMSKSKGNVIPLRKAIEEYGADVVRLY 603
DALR_2 pfam09190
DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.
274-310 1.85e-03

DALR domain; This DALR domain is found in cysteinyl-tRNA-synthetases.


Pssm-ID: 462711 [Multi-domain]  Cd Length: 63  Bit Score: 36.41  E-value: 1.85e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1907191153 274 AVKAALANDFDTPRAVNTILDLVHHANRQLRAVSKEA 310
Cdd:pfam09190   1 KFIEAMDDDFNTPEALAVLFELAKEINRALKTNDAEA 37
tRNA-synt_1 pfam00133
tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too ...
186-225 2.36e-03

tRNA synthetases class I (I, L, M and V); Other tRNA synthetase sub-families are too dissimilar to be included.


Pssm-ID: 459685 [Multi-domain]  Cd Length: 602  Bit Score: 40.09  E-value: 2.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1907191153 186 KMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIEYS 225
Cdd:pfam00133 563 KMSKSLGNVIDPLDVIDKYGADALRLWLANSDYGRDINLS 602
tRNA-synt_1f pfam01921
tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from ...
185-223 5.16e-03

tRNA synthetases class I (K); This family includes only lysyl tRNA synthetases from prokaryotes.


Pssm-ID: 396483  Cd Length: 357  Bit Score: 38.78  E-value: 5.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1907191153 185 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYRSAIE 223
Cdd:pfam01921 278 GKMSSSKGNVITPEDWLEYAPPESLRFLMFRTKPKKAKD 316
PLN02959 PLN02959
aminoacyl-tRNA ligase
168-214 5.19e-03

aminoacyl-tRNA ligase


Pssm-ID: 215518 [Multi-domain]  Cd Length: 1084  Bit Score: 39.28  E-value: 5.19e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907191153  168 WGNYFLHSGHLHVKGteEKMSKSLKNYITIKDFLKTFSPDVFRlFCL 214
Cdd:PLN02959   702 WPRGFRCNGHLMLNS--EKMSKSTGNFLTLRQAIEEFSADATR-FAL 745
IleRS_core cd00818
catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases ...
185-219 5.60e-03

catalytic core domain of isoleucyl-tRNA synthetases; Isoleucine amino-acyl tRNA synthetases (IleRS) catalytic core domain . This class I enzyme is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. IleRS has an insertion in the core domain, which is subject to both deletions and rearrangements. This editing region hydrolyzes mischarged cognate tRNAs and thus prevents the incorporation of chemically similar amino acids.


Pssm-ID: 173909 [Multi-domain]  Cd Length: 338  Bit Score: 38.75  E-value: 5.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1907191153 185 EKMSKSLKNYITIKDFLKTFSPDVFRLFCLRTNYR 219
Cdd:cd00818   298 RKMSKSLGNYVDPQEVVDKYGADALRLWVASSDVY 332
 
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