|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-426 |
0e+00 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 618.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 2 AKQIQAVRGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEvtDIVEKEMYTFADRNGDLLTLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 82 PEGTAVCVRAGNQNGLLYNQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGITEhV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKD-F 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 162 RLELNSLGSNEARADyrdALVAYLE-----QHIDVLDEDSKRRMYSNPLR-VLDSKNPDVQAILTDAPKLSENLDAESKE 235
Cdd:COG0124 158 TLEINSRGLPEERAE---ALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 236 HFANLCERLDAAGVSYTVNEKLVRGLDYYNRTVFEWVTDSLGAQGTVCAGGRYDGLVEQLGGKATPAVGFAMGLERLVLL 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 316 LQALECVGDIRRNADVYLAAMGDKASIQAPAIAAQLRKDvpGLRVMVHAGGGNFKKQLKRADKSDALVAVIIGEDELEKG 395
Cdd:COG0124 315 LEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420 430
....*....|....*....|....*....|.
gi 639360634 396 VVTIKYLRERkEQVTLELEQAKALLAELING 426
Cdd:COG0124 393 TVTLKDLATG-EQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-413 |
0e+00 |
|
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed genome. Apparent second copies from Bacillus subtilis, Synechocystis sp., and Aquifex aeolicus are slightly shorter, more closely related to each other than to other hisS proteins, and actually serve as regulatory subunits for an enzyme of histidine biosynthesis. They were excluded from the seed alignment and score much lower than do single copy histidyl-tRNA synthetases of other genomes not included in the seed alignment. These putative second copies of HisS score below the trusted cutoff. The regulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c), and related proteins from other species designated eIF-2 alpha kinase, have a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his), an indicator of amino acid starvation; these regulatory proteins are not orthologous and so score below the noise cutoff. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273080 [Multi-domain] Cd Length: 404 Bit Score: 609.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 6 QAVRGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDIVEKEMYTFADRNGDLLTLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 86 AVCVRAGNQNGLLYNQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGITeHVRLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLK-DFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 166 NSLGSNEARADYRDALVAYLEQHIDVLDEDSKRRMYSNPLRVLDSKNPDVQAILTDAPKLSENLDAESKEHFANLCERLD 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 246 AAGVSYTVNEKLVRGLDYYNRTVFEWVTDSLGAQGTVCAGGRYDGLVEQLGGKATPAVGFAMGLERLVLLLQALECVGDI 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 326 RRNADVYLAAMGDKASIQAPAIAAQLRKDvpGLRVMVHAGGGNFKKQLKRADKSDALVAVIIGEDELEKGVVTIKYLRER 405
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*...
gi 639360634 406 kEQVTLEL 413
Cdd:TIGR00442 398 -EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-408 |
1.04e-144 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 418.92 E-value: 1.04e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 1 MAKqIQAVRGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDIVEKEMYTFADRNGDLLTL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 81 RPEGTAVCVRAGNQNGLLY-NQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGItE 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQV-K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 160 HVRLELNSLGSNEARADYRDALVAYLEQHIDVLDEDSKRRMYSNPLRVLDSKNPDVQAILTDAPKLSENLDAESKEHFAN 239
Cdd:CHL00201 159 NLILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 240 LCERLDAAGVSYTVNEKLVRGLDYYNRTVFEWVTDSLGAQGTVCAGGRYDGLVEQLGGKATPAVGFAMGLERlvLLLQAL 319
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLER--LLLIAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 320 ECVGDIRRNADVYLAAMGDKASIQAPAIAAQLRKDVpgLRVMVHAGGGNFKKQLKRADKSDALVAVIIGEDELEKGVVTI 399
Cdd:CHL00201 317 DNIILPKQSIDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITI 394
|
....*....
gi 639360634 400 KYLRERKEQ 408
Cdd:CHL00201 395 KWLDEQVQE 403
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-317 |
3.40e-97 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 291.43 E-value: 3.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 18 DTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGevtDIVEKEMYTFADRNGDLLTLRPEGTAVCVRAGNQNGL 97
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSG---DEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 98 LYNQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGITeHVRLELNSLGSNEA---- 173
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLK-DFQIKINHRGILDGiagl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 174 ---RADYRDALVAYLEQhidvldedskrrmysnplrvldsknpdvqailtdapklsenldaESKEHFANLCERLDAAGV- 249
Cdd:cd00773 157 ledREEYIERLIDKLDK--------------------------------------------EALAHLEKLLDYLEALGVd 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639360634 250 -SYTVNEKLVRGLDYYNRTVFEWVTDSLGAQGTVCAGGRYDGLVEQLGGKATPAVGFAMGLERLVLLLQ 317
Cdd:cd00773 193 iKYSIDLSLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
9.56e-35 |
|
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.
Pssm-ID: 433170 [Multi-domain] Cd Length: 309 Bit Score: 130.78 E-value: 9.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 10 GMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDivekEMYTFADRNGDLLTLRPEGTAVCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 90 R--AGNQNGllyNQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGItEHVRLELNS 167
Cdd:pfam13393 77 RidAHRLNR---PGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV-PGVTLDLGH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 168 -------LGSNEARADYRDALVAYLEQH----IDVLDEDSK-RRMYSNPLRVLDSKNPDVQAILTDAPKLSENLDA-ESK 234
Cdd:pfam13393 153 vglvralLEAAGLSEALEEALRAALQRKdaaeLAELAAEAGlPPALRRALLALPDLYGGPEVLDEARAALPGLPALqEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 235 EHFANLCERLDAAG--VSYTVNEKLVRGLDYYNRTVFEWVTDslGAQGTVCAGGRYDGLVEQLgGKATPAVGFAMGLERL 312
Cdd:pfam13393 233 DELEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYAP--GVGEPLARGGRYDDLGAAF-GRARPATGFSLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-426 |
0e+00 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 618.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 2 AKQIQAVRGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEvtDIVEKEMYTFADRNGDLLTLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 82 PEGTAVCVRAGNQNGLLYNQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGITEhV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKD-F 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 162 RLELNSLGSNEARADyrdALVAYLE-----QHIDVLDEDSKRRMYSNPLR-VLDSKNPDVQAILTDAPKLSENLDAESKE 235
Cdd:COG0124 158 TLEINSRGLPEERAE---ALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 236 HFANLCERLDAAGVSYTVNEKLVRGLDYYNRTVFEWVTDSLGAQGTVCAGGRYDGLVEQLGGKATPAVGFAMGLERLVLL 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 316 LQALECVGDIRRNADVYLAAMGDKASIQAPAIAAQLRKDvpGLRVMVHAGGGNFKKQLKRADKSDALVAVIIGEDELEKG 395
Cdd:COG0124 315 LEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420 430
....*....|....*....|....*....|.
gi 639360634 396 VVTIKYLRERkEQVTLELEQAKALLAELING 426
Cdd:COG0124 393 TVTLKDLATG-EQETVPLDELVEYLKELLAE 422
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-413 |
0e+00 |
|
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed genome. Apparent second copies from Bacillus subtilis, Synechocystis sp., and Aquifex aeolicus are slightly shorter, more closely related to each other than to other hisS proteins, and actually serve as regulatory subunits for an enzyme of histidine biosynthesis. They were excluded from the seed alignment and score much lower than do single copy histidyl-tRNA synthetases of other genomes not included in the seed alignment. These putative second copies of HisS score below the trusted cutoff. The regulatory protein kinase GCN2 of Saccharomyces cerevisiae (YDR283c), and related proteins from other species designated eIF-2 alpha kinase, have a domain closely related to histidyl-tRNA synthetase that may serve to detect and respond to uncharged tRNA(his), an indicator of amino acid starvation; these regulatory proteins are not orthologous and so score below the noise cutoff. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273080 [Multi-domain] Cd Length: 404 Bit Score: 609.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 6 QAVRGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDIVEKEMYTFADRNGDLLTLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 86 AVCVRAGNQNGLLYNQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGITeHVRLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLK-DFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 166 NSLGSNEARADYRDALVAYLEQHIDVLDEDSKRRMYSNPLRVLDSKNPDVQAILTDAPKLSENLDAESKEHFANLCERLD 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 246 AAGVSYTVNEKLVRGLDYYNRTVFEWVTDSLGAQGTVCAGGRYDGLVEQLGGKATPAVGFAMGLERLVLLLQALECVGDI 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 326 RRNADVYLAAMGDKASIQAPAIAAQLRKDvpGLRVMVHAGGGNFKKQLKRADKSDALVAVIIGEDELEKGVVTIKYLRER 405
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*...
gi 639360634 406 kEQVTLEL 413
Cdd:TIGR00442 398 -EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-408 |
1.04e-144 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 418.92 E-value: 1.04e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 1 MAKqIQAVRGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDIVEKEMYTFADRNGDLLTL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 81 RPEGTAVCVRAGNQNGLLY-NQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGItE 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQV-K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 160 HVRLELNSLGSNEARADYRDALVAYLEQHIDVLDEDSKRRMYSNPLRVLDSKNPDVQAILTDAPKLSENLDAESKEHFAN 239
Cdd:CHL00201 159 NLILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 240 LCERLDAAGVSYTVNEKLVRGLDYYNRTVFEWVTDSLGAQGTVCAGGRYDGLVEQLGGKATPAVGFAMGLERlvLLLQAL 319
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLER--LLLIAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 320 ECVGDIRRNADVYLAAMGDKASIQAPAIAAQLRKDVpgLRVMVHAGGGNFKKQLKRADKSDALVAVIIGEDELEKGVVTI 399
Cdd:CHL00201 317 DNIILPKQSIDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITI 394
|
....*....
gi 639360634 400 KYLRERKEQ 408
Cdd:CHL00201 395 KWLDEQVQE 403
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-317 |
3.40e-97 |
|
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. It is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ. HisZ along with HisG catalyze the first reaction in histidine biosynthesis. HisZ is found only in a subset of bacteria and differs from HisRS in lacking a C-terminal anti-codon binding domain.
Pssm-ID: 238396 [Multi-domain] Cd Length: 261 Bit Score: 291.43 E-value: 3.40e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 18 DTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGevtDIVEKEMYTFADRNGDLLTLRPEGTAVCVRAGNQNGL 97
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSG---DEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 98 LYNQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGITeHVRLELNSLGSNEA---- 173
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLK-DFQIKINHRGILDGiagl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 174 ---RADYRDALVAYLEQhidvldedskrrmysnplrvldsknpdvqailtdapklsenldaESKEHFANLCERLDAAGV- 249
Cdd:cd00773 157 ledREEYIERLIDKLDK--------------------------------------------EALAHLEKLLDYLEALGVd 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639360634 250 -SYTVNEKLVRGLDYYNRTVFEWVTDSLGAQGTVCAGGRYDGLVEQLGGKATPAVGFAMGLERLVLLLQ 317
Cdd:cd00773 193 iKYSIDLSLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
13-317 |
4.65e-48 |
|
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA synthetase, found in Bacillus subtilis, Synechocystis sp., Aquifex aeolicus, and others, are in fact a regulatory subunit of ATP phosphoribosyltransferase, and usually encoded by a gene adjacent to that encoding the catalytic subunit. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273081 [Multi-domain] Cd Length: 313 Bit Score: 166.64 E-value: 4.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 13 DCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGevtdIVEKEMYTFADRNGDLLTLRPEGTAVCVRAG 92
Cdd:TIGR00443 2 DLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSG----ILNEDLFKLFDQLGRVLGLRPDMTAPIARLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 93 NQNGLLYNQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGITE------HV---RL 163
Cdd:TIGR00443 78 STRLRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDfkielgHVglvRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 164 ELNSLG-SNEARADYRDALVAY----LEQHIDVLDEDSKRRMYSNPLRVLDSKNPDVqaiLTDAPKLSENLDAE-SKEHF 237
Cdd:TIGR00443 158 LLEEAGlPEEAREALREALARKdlvaLEELVAELGLSPEVRERLLALPRLRGDGEEV---LEEARALAGSETAEaALDEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 238 ANLCERLDAAGVS--YTVNEKLVRGLDYYNRTVFEWVTDSLGAqgTVCAGGRYDGLVEQLgGKATPAVGFAMGLERLVLL 315
Cdd:TIGR00443 235 EAVLELLEARGVEeyISLDLGLVRGYHYYTGLIFEGYAPGLGA--PLAGGGRYDELLGRF-GRPLPATGFALNLERLLEA 311
|
..
gi 639360634 316 LQ 317
Cdd:TIGR00443 312 LT 313
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
1-363 |
6.55e-42 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 152.33 E-value: 6.55e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 1 MAKQIQAvrGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGevtDIVEKEMYTFADR-NGDLLT 79
Cdd:PRK12292 1 MMWQLPE--GIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGG---AILDLRTFKLVDQlSGRTLG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 80 LRPEGTAVCVRAgnQNGLLYNQE--QRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGI 157
Cdd:PRK12292 76 LRPDMTAQIARI--AATRLANRPgpLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 158 tEHVRLEL-----------NSLGSNEARADYRDAL----VAYLEQHIDVLDEDSKRRMysnpLRVLDSKNPDvqAILTDA 222
Cdd:PRK12292 154 -PNFTLDLghvglfralleAAGLSEELEEVLRRALankdYVALEELVLDLSEELRDAL----LALPRLRGGR--EVLEEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 223 PKLSENLDA-ESKEHFANLCERLDAAGVSYTVNEKL--VRGLDYYNRTVFEWVTDSLGAQgtVCAGGRYDGLVEQLgGKA 299
Cdd:PRK12292 227 RKLLPSLPIkRALDELEALAEALEKYGYGIPLSLDLglLRHLDYYTGIVFEGYVDGVGNP--IASGGRYDDLLGRF-GRA 303
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639360634 300 TPAVGFAMGLERLVLLLQALEcvgdiRRNADVYLAAMGDKASIQAPAIAAQLRKDvpGLRVMVH 363
Cdd:PRK12292 304 RPATGFSLDLDRLLELQLELP-----VEARKDLVIAPDSEALAAALAAAQELRKK--GEIVVLA 360
|
|
| Gly_His_Pro_Ser_Thr_tRS_core |
cd00670 |
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic ... |
18-317 |
2.46e-40 |
|
Gly_His_Pro_Ser_Thr_tRNA synthetase class II core domain. This domain is the core catalytic domain of tRNA synthetases of the subgroup containing glycyl, histidyl, prolyl, seryl and threonyl tRNA synthetases. It is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. These enzymes belong to class II aminoacyl-tRNA synthetases (aaRS) based upon their structure and the presence of three characteristic sequence motifs in the core domain. This domain is also found at the C-terminus of eukaryotic GCN2 protein kinase and at the N-terminus of the ATP phosphoribosyltransferase accessory subunit, HisZ and the accessory subunit of mitochondrial polymerase gamma (Pol gamma b) . Most class II tRNA synthetases are dimers, with this subgroup consisting of mostly homodimers. These enzymes attach a specific amino acid to the 3' OH group of ribose of the appropriate tRNA.
Pssm-ID: 238359 [Multi-domain] Cd Length: 235 Bit Score: 143.69 E-value: 2.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 18 DTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIgeVTDIVEKEMYTFADRNGDL----LTLRPEGTAVCVRAGN 93
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG--HLDGYRKEMYTFEDKGRELrdtdLVLRPAACEPIYQIFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 94 QNGLLY-NQEQRLWYMGPMFRHERPQ---KGRYRQFHQFGLETFGIATA--DIDAEVILLTAQLWEAFGitEHVRLELNS 167
Cdd:cd00670 79 GEILSYrALPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGEPEEaeEERREWLELAEEIARELG--LPVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 168 LGSNEARADyrdalvayleqhidvldedskrrmysnplrvldsknpdvqailtdapklsenldaeskehfanlcerldaa 247
Cdd:cd00670 157 DPFFGRGGK----------------------------------------------------------------------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 248 gvsytvneklvRGLDYYNRTVFEWVTDSL--GAQGTVCAGGRYDGLVEQ---------LGGKATPAVGFAMGLERLVLLL 316
Cdd:cd00670 166 -----------RGLDAGRETVVEFELLLPlpGRAKETAVGSANVHLDHFgasfkidedGGGRAHTGCGGAGGEERLVLAL 234
|
.
gi 639360634 317 Q 317
Cdd:cd00670 235 L 235
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
5-412 |
3.11e-39 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 147.20 E-value: 3.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 5 IQAVRGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGE-VTDivekEMYTFADRNGDLLTLRPE 83
Cdd:PLN02530 70 VNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEeITD----QLYNFEDKGGRRVALRPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 84 GTAVCVRAGNQNGllynQEQRL---WY-MGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGIT- 158
Cdd:PLN02530 146 LTPSLARLVLQKG----KSLSLplkWFaIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGITs 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 159 EHVRLELNS---LGSNEARADYRDALVAYLEQHIDVLDEdSKRRMYSNPLRVLDSKNPDVQAIL-----TDAPKLSENLD 230
Cdd:PLN02530 222 SDVGIKVSSrkvLQAVLKSYGIPEESFAPVCVIVDKLEK-LPREEIEKELDTLGVSEEAIEGILdvlslKSLDDLEALLG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 231 AESkEHFANLcERLDAAGVSYTVNEKL------VRGLDYYNRTVFEWVtDSLGAQGTVCAGGRYDGLVEQLGGKATPAVG 304
Cdd:PLN02530 301 ADS-EAVADL-KQLFSLAEAYGYQDWLvfdasvVRGLAYYTGIVFEGF-DRAGKLRAICGGGRYDRLLSTFGGEDTPACG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 305 FAMGLERLVLLLQALECVGDIRRNADVYLAAMGDKASIQAPAIAAQLRKDvpGLRVMVHAGGGNFKKQLKRADKSDALVA 384
Cdd:PLN02530 378 FGFGDAVIVELLKEKGLLPELPHQVDDVVFALDEDLQGAAAGVASRLREK--GRSVDLVLEPKKLKWVFKHAERIGAKRL 455
|
410 420
....*....|....*....|....*....
gi 639360634 385 VIIGEDELEKGVVTIKYLRERKE-QVTLE 412
Cdd:PLN02530 456 VLVGASEWERGMVRVKDLSSGEQtEVKLD 484
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
15-318 |
8.49e-39 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 141.85 E-value: 8.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 15 LPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDiveKEMYTFADRNGDLLTLRPEGTAVCVR-AGN 93
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVARiAAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 94 qngLLYNQE--QRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGITE------HVRLeL 165
Cdd:COG3705 78 ---RLANRPgpLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDftldlgHVGL-F 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 166 NSL-----GSNEARADYRDAL----VAYLEQHIDVLDEDSK-RRMYsnpLRVLDSKNPDvqAILTDAPKLSENLDAES-K 234
Cdd:COG3705 154 RALlealgLSEEQREELRRALarkdAVELEELLAELGLSEElAEAL---LALPELYGGE--EVLARARALLLDAAIRAaL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 235 EHFANLCERLDAAG--VSYTVNEKLVRGLDYYNRTVFEWVTDSLGaqGTVCAGGRYDGLVEQLGgKATPAVGFAMGLERL 312
Cdd:COG3705 229 DELEALAEALAARGpdVRLTFDLSELRGYDYYTGIVFEAYAPGVG--DPLARGGRYDGLLAAFG-RARPATGFSLDLDRL 305
|
....*.
gi 639360634 313 VLLLQA 318
Cdd:COG3705 306 LRALPA 311
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
9.56e-35 |
|
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP phosphoribosyltransferase regulatory subunits.
Pssm-ID: 433170 [Multi-domain] Cd Length: 309 Bit Score: 130.78 E-value: 9.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 10 GMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDivekEMYTFADRNGDLLTLRPEGTAVCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 90 R--AGNQNGllyNQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGItEHVRLELNS 167
Cdd:pfam13393 77 RidAHRLNR---PGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV-PGVTLDLGH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 168 -------LGSNEARADYRDALVAYLEQH----IDVLDEDSK-RRMYSNPLRVLDSKNPDVQAILTDAPKLSENLDA-ESK 234
Cdd:pfam13393 153 vglvralLEAAGLSEALEEALRAALQRKdaaeLAELAAEAGlPPALRRALLALPDLYGGPEVLDEARAALPGLPALqEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 235 EHFANLCERLDAAG--VSYTVNEKLVRGLDYYNRTVFEWVTDslGAQGTVCAGGRYDGLVEQLgGKATPAVGFAMGLERL 312
Cdd:pfam13393 233 DELEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYAP--GVGEPLARGGRYDDLGAAF-GRARPATGFSLDLEAL 309
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
4-408 |
1.73e-33 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 129.85 E-value: 1.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 4 QIQAVRGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDIVeKEMYTFADRNGDLLTLRPE 83
Cdd:PRK12420 3 EMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGDEIL-KEIYTLTDQGKRDLALRYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 84 GT----AVCVragnqngllYNQEQRLWY----MGPMFRHERPQKGRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAF 155
Cdd:PRK12420 82 LTipfaKVVA---------MNPNIRLPFkryeIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 156 GITEHVRLE--------LNSLGSNEARADyrDALVAY--LEQ-HIDVLDEDSKRRMYSNPL--RVLDSKNPDVQAILTD- 221
Cdd:PRK12420 153 NLEVTIQYNnrkllngiLQAIGIPTELTS--DVILSLdkIEKiGIDGVRKDLLERGISEEMadTICNTVLSCLQLSIADf 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 222 APKLSENLDAESKEHFANLCERLDAAGVS--YTVNEKLVRGLDYYNRTVFEwVTDSLGA-QGTVCAGGRYDGLVEQLGGK 298
Cdd:PRK12420 231 KEAFNNPLVAEGVNELQQLQQYLIALGINenCIFNPFLARGLTMYTGTVYE-IFLKDGSiTSSIGSGGRYDNIIGAFRGD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 299 --ATPAVGFAMGLErlvLLLQALECVGDIRRNADVYLAAMGDKAsiQAPAIAAQLRKDvPGLRVMVHAGGGNFKKQLKRA 376
Cdd:PRK12420 310 dmNYPTVGISFGLD---VIYTALSQKETISSTADVFIIPLGTEL--QCLQIAQQLRST-TGLKVELELAGRKLKKALNYA 383
|
410 420 430
....*....|....*....|....*....|..
gi 639360634 377 DKSDALVAVIIGEDELEKGVVTIKYLRERKEQ 408
Cdd:PRK12420 384 NKENIPYVLIIGEEEVSTGTVMLRNMKEGSEV 415
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
9-425 |
8.28e-29 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 119.22 E-value: 8.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 9 RGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDIVekemYTFADRNGDLLTLRPEGTAVC 88
Cdd:PLN02972 331 KGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLI----YDLADQGGELCSLRYDLTVPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 89 VRAGNQNGLlynQEQRLWYMGPMFRHERPQKGRYRQFHQFGLETFGI-ATADIDAEVILLTAQLWEafgitehvrlELNs 167
Cdd:PLN02972 407 ARYVAMNGI---TSFKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVyEPMGPDFEIIKVLTELLD----------ELD- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 168 LGSNEARADYRDALVAYLE-------------QHIDVLDEDS----KRRMYSNplRVLDSKNPD---------------V 215
Cdd:PLN02972 473 IGTYEVKLNHRKLLDGMLEicgvppekfrticSSIDKLDKQSfeqvKKEMVEE--KGLSNETADkignfvkergpplelL 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 216 QAILTDAPKLSEN-LDAESKEHFANLCERLDAAGVSYTV--NEKLVRGLDYYNRTVFEWVTdsLGAQ-GTVCAGGRYDGL 291
Cdd:PLN02972 551 SKLRQEGSEFLGNaSSRAALDELEIMFKALEKSKAIGKIvfDLSLARGLDYYTGVIYEAVF--KGAQvGSIAAGGRYDNL 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 292 VEQLGGKATPAVGFAMGLERLVLLLQALECV--GDIR-RNADVYLAAMGDKASIQAPAIAAQLRKdvPGLRVMvHAGGGN 368
Cdd:PLN02972 629 VGMFSGKQVPAVGVSLGIERVFAIMEQQEEEksQVIRpTETEVLVSIIGDDKLALAAELVSELWN--AGIKAE-YKVSTR 705
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 639360634 369 FKKQLKRADKSDALVAVIIGEDELEKGVVTIKYLRERKEQVTLELEQAKALLAELIN 425
Cdd:PLN02972 706 KAKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELLK 762
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
21-170 |
3.96e-28 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 110.29 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 21 VWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEvtdivEKEMYTFADRNGDLLTLRPEGTAVCVRAGNQNglLYN 100
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE-----PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSH--IRK 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 639360634 101 QEQRLWYMGPMFRHERPQKG--RYRQFHQFGLETFG--IATADIDAEVILLTAQLWEAFGITEHVRLELNSLGS 170
Cdd:cd00768 74 LPLRLAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGedGEEASEFEELIELTEELLRALGIKLDIVFVEKTPGE 147
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
329-421 |
1.13e-23 |
|
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases (aaRS). This alignment contains the anticodon binding domain, which is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only.
Pssm-ID: 238436 [Multi-domain] Cd Length: 91 Bit Score: 94.14 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 329 ADVYLAAMGDKASIQAPAIAAQLRKDvpGLRVMVHAGGGNFKKQLKRADKSDALVAVIIGEDELEKGVVTIKYLrERKEQ 408
Cdd:cd00859 2 VDVYVVPLGEGALSEALELAEQLRDA--GIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDL-ETGEQ 78
|
90
....*....|...
gi 639360634 409 VTLELEQAKALLA 421
Cdd:cd00859 79 ETVALDELVEELK 91
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
68-318 |
9.50e-21 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 89.01 E-value: 9.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 68 YTFADRNGDLLTLRPEGTAVCVRAGNQNGL-LYNQEQRLWYMGPMFRHERP--QKG--RYRQFHQFGLETFGIATA--DI 140
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLrSKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHAPGQspDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 141 DAEVILLTAQLWEAFGITEHVRLELNSLGSnearadyrdalvayleqhidvldedskrrmysnplrvldsknpdvqailt 220
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGS-------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 221 dapklsenldaeskehfanlcerldaagvsytvneklvrgLDYYNRTVFEWVTDSLGAQG-TVCAGGRYDGLVEQLGGKA 299
Cdd:pfam00587 111 ----------------------------------------AFYGPKLDFEVVFPSLGKQRqTGTIQNDGFRLPRRLGIRY 150
|
250 260
....*....|....*....|....*....
gi 639360634 300 --------TP-AVGFA-MGLERLVLLLQA 318
Cdd:pfam00587 151 kdedneskFPyMIHRAgLGVERFLAAILE 179
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
29-312 |
2.84e-16 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 79.98 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 29 LRETVASFGYQEIRFPIVESTDLFKRSIGEvtDIvEKEMYTFADRNGDLLTLRPEGT-AVCVRAGNQNGllyNQEQRLWY 107
Cdd:PRK12295 14 LLASFEAAGAVRVDPPILQPAEPFLDLSGE--DI-RRRIFVTSDENGEELCLRPDFTiPVCRRHIATAG---GEPARYAY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 108 MGPMFRHerpQKGRYRQFHQFGLETFG-IATADIDAEVILLTAQLWEAFGITE-HVRLE--------LNSLGSNEA---- 173
Cdd:PRK12295 88 LGEVFRQ---RRDRASEFLQAGIESFGrADPAAADAEVLALALEALAALGPGDlEVRLGdvglfaalVDALGLPPGwkrr 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 174 ------RADYRDALVAYL--------EQHIDVL----DEDSKRRMYSNPL------------------RVL--------D 209
Cdd:PRK12295 165 llrhfgRPRSLDALLARLagprvdplDEHAGVLaalaDEAAARALVEDLMsiagispvggrspaeiarRLLekaalaaaA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 210 SKNPDVQAILTDAPKLSENLDAESK-----------------EHFANLCERLDAAGVSYtvnEKLV------RGLDYYNR 266
Cdd:PRK12295 245 RLPAEALAVLERFLAISGPPDAALAalralaadagldldaalDRFEARLAALAARGIDL---ERLRfsasfgRPLDYYTG 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 639360634 267 TVFEwVTDSLGAQGTVCAGGRYDGLVEQLG-GKATPAVGFAMGLERL 312
Cdd:PRK12295 322 FVFE-IRAAGNGDPPLAGGGRYDGLLTRLGaGEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
330-423 |
4.11e-11 |
|
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA synthetases it is probably the anticodon binding domain.
Pssm-ID: 460819 [Multi-domain] Cd Length: 94 Bit Score: 59.14 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 330 DVYLAAMGDKASIQAPA---IAAQLRKDvpGLRVMVHAGGGNFKKQLKRADKSDALVAVIIGEDELEKGVVTIKYlRERK 406
Cdd:pfam03129 1 QVVVIPLGEKAEELEEYaqkLAEELRAA--GIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRR-RDTG 77
|
90
....*....|....*..
gi 639360634 407 EQVTLELEQAKALLAEL 423
Cdd:pfam03129 78 EQETVSLDELVEKLKEL 94
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
10-361 |
6.43e-10 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 60.37 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 10 GMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSIGEVTDIVekemyTF--ADR-NGDLLTLRPEGTA 86
Cdd:PRK12421 12 GVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQ-----TFklIDQlSGRLMGVRADITP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 87 VCVRAgnqNGLLYNQE--QRLWYMGPMFrHERPQK-GRYRQFHQFGLETFGIATADIDAEVILLTAQLWEAFGItEHVRL 163
Cdd:PRK12421 87 QVARI---DAHLLNREgvARLCYAGSVL-HTLPQGlFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGV-PALHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 164 ELNSLG-----------SNEARADYRDAL----VAYLEQHIDVLDEDSK-RRMysnpLRVLDSKNPDVQAILTDAPKLSE 227
Cdd:PRK12421 162 DLGHVGifrrlaelaglSPEEEEELFDLLqrkaLPELAEVCQNLGVGSDlRRM----FYALARLNGGLEALDRALSVLAL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 228 NLDA------ESKEHFANLCERLDAAGVSYTVNEklVRGLDYYNRTVFEWVTDSLGAQgtVCAGGRYDGlVEQLGGKATP 301
Cdd:PRK12421 238 QDAAirqaldELKTLAAHLKNRWPELPVSIDLAE--LRGYHYHTGLVFAAYIPGRGQA--LARGGRYDG-IGEAFGRARP 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 302 AVGFAMGLERLVLLLQALECVGDIrrnadvYLAAMGDKASIQApaiAAQLRKDvpGLRVM 361
Cdd:PRK12421 313 ATGFSMDLKELLALQFLEEEAGAI------LAPWGDDPDLLAA---IAELRQQ--GERVV 361
|
|
| ProRS_core_prok |
cd00779 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
21-125 |
2.56e-06 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain. This subfamily contains the core domain of ProRS from prokaryotes and from the mitochondria of eukaryotes.
Pssm-ID: 238402 [Multi-domain] Cd Length: 255 Bit Score: 48.34 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 21 VWQKVENILRETVASFGYQEIRFPIVESTDLFKRSiGEVtDIVEKEMYTFADRNGDLLTLRPEGTAVCVRAGNQNGLLYN 100
Cdd:cd00779 33 VLKKIENIIREEMNKIGAQEILMPILQPAELWKES-GRW-DAYGPELLRLKDRHGKEFLLGPTHEEVITDLVANEIKSYK 110
|
90 100
....*....|....*....|....*....
gi 639360634 101 Q-EQRLWYMGPMFRHE-RPQKG--RYRQF 125
Cdd:cd00779 111 QlPLNLYQIQTKFRDEiRPRFGlmRGREF 139
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
330-420 |
8.11e-06 |
|
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and prolyl tRNA synthetases, which are classified as a group of class II aminoacyl-tRNA synthetases (aaRS). In aaRSs, the anticodon binding domain is responsible for specificity in tRNA-binding, so that the activated amino acid is transferred to a ribose 3' OH group of the appropriate tRNA only. This domain is also found in the accessory subunit of mitochondrial polymerase gamma (Pol gamma b).
Pssm-ID: 238379 [Multi-domain] Cd Length: 94 Bit Score: 43.93 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 330 DVYLAAMGDKaSIQAPAIAAQLRKDV--PGLRVMVHAGGGNFKKQLKRADKSDALVAVIIGEDELEKGVVTIKyLRERKE 407
Cdd:cd00738 3 DVAIVPLTDP-RVEAREYAQKLLNALlaNGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVK-SRDTGE 80
|
90
....*....|...
gi 639360634 408 QVTLELEQAKALL 420
Cdd:cd00738 81 SETLHVDELPEFL 93
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
15-181 |
1.67e-05 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 46.39 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 15 LPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSigEVTDIVEKEMYTFaDRNGDLLTLRPegtAVCVragnq 94
Cdd:cd00771 26 LPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWETS--GHWDHYRENMFPF-EEEDEEYGLKP---MNCP----- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 95 nG--LLYNQEQRLWY--------MGPMFRHErpQKG------RYRQFHQFGLETFgiATAD-IDAE---VILLTAQLWEA 154
Cdd:cd00771 95 -GhcLIFKSKPRSYRdlplrlaeFGTVHRYE--QSGalhgltRVRGFTQDDAHIF--CTPDqIKEEikgVLDLIKEVYSD 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 639360634 155 FGITEHvRLEL-----NSLGSNE----ARADYRDAL 181
Cdd:cd00771 170 FGFFDY-KVELstrpeKFIGSDEvwekAEAALREAL 204
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
8-125 |
2.56e-04 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 42.36 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639360634 8 VRGMNDCLPGDTQVWQKVENILRETVASFGYQEIRFPIVESTDLFKRSiGEVTDIVEKEMYTFADRNGDL----LTLRPE 83
Cdd:cd00772 21 GRGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKE-AEHDEGFSKELAVFKDAGDEEleedFALRPT 99
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 639360634 84 GTAVCVRAGNQNGLLYNQ-EQRLWYMGPMFRHE-RPQKG--RYRQF 125
Cdd:cd00772 100 LEENIGEIAAKFIKSWKDlPQHLNQIGNKFRDEiRPRFGflRAREF 145
|
|
| |
