|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-424 |
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: 641.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 2 AKNIQAIRGMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEvtDVVEKEMYTFEDRNGESLTLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 82 PEGTAGCVRAGIEHGLLYNQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL-KDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 162 KLELNSIGSLEARAnyrDALVAFLE-----QHVEVLDEDCKRRMYSNPLR-VLDSKNPEVQALLNDAPRLSEYLDEESRA 235
Cdd:COG0124 158 TLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 236 HFAGLCELLAQAGIPYTVNERLVRGLDYYNRTVFEWVTTSLGAQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLL 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 316 VQAVNPEFKAPSAIDVYVISSGAGTQSAAMRLAEQVRDAapQLKLMTNYGGGNFKKQITRADKWGARIALILGESEVAAQ 395
Cdd:COG0124 315 LEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420
....*....|....*....|....*....
gi 896334556 396 QVVVKDLRSGEQETLAQSEVAARLALMLG 424
Cdd:COG0124 393 TVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-412 |
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: 631.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 6 QAIRGMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGESLTLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 86 AGCVRAGIEHGLLYNQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHVKLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL-KDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 166 NSIGSLEARANYRDALVAFLEQHVEVLDEDCKRRMYSNPLRVLDSKNPEVQALLNDAPRLSEYLDEESRAHFAGLCELLA 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 246 QAGIPYTVNERLVRGLDYYNRTVFEWVTTSLGAQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQAVNPEFKA 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 326 PSAIDVYVISSGAGTQSAAMRLAEQVRDAApqLKLMTNYGGGNFKKQITRADKWGARIALILGESEVAAQQVVVKDLRSG 405
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKAG--IRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
gi 896334556 406 EQETLAQ 412
Cdd:TIGR00442 398 EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-414 |
4.85e-148 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 427.39 E-value: 4.85e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 1 MAKnIQAIRGMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGESLTL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 81 RPEGTAGCVRAGIEHGLLY-NQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaE 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQV-K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 160 HVKLELNSIGSLEARANYRDALVAFLEQHVEVLDEDCKRRMYSNPLRVLDSKNPEVQALLNDAPRLSEYLDEESRAHFAG 239
Cdd:CHL00201 159 NLILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 240 LCELLAQAGIPYTVNERLVRGLDYYNRTVFEWVTTSLGAQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ-- 317
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKdn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 318 AVNPEFKapsaIDVYVISSGAGTQSAAMRLAEQVRDAapQLKLMTNYGGGNFKKQITRADKWGARIALILGESEVAAQQV 397
Cdd:CHL00201 319 IILPKQS----IDVYIATQGLKAQKKGWEIIQFLEKQ--NIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCI 392
|
410
....*....|....*..
gi 896334556 398 VVKDLRSGEQETLAQSE 414
Cdd:CHL00201 393 TIKWLDEQVQENAQYSN 409
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-317 |
3.65e-104 |
|
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: 309.15 E-value: 3.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 18 ETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRaigEVTDVVEKEMYTFEDRNGESLTLRPEGTAGCVRAGIEHGL 97
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLR---KSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 98 LYNQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHVKLELNSIGSLEARANy 177
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL-KDFQIKINHRGILDGIAG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 178 rdalvafleqhvevldedckrrmysnplrvlDSKNPEVQALlndapRLSEYLDEESRAHFAGLCELLAQAG--IPYTVNE 255
Cdd:cd00773 156 -------------------------------LLEDREEYIE-----RLIDKLDKEALAHLEKLLDYLEALGvdIKYSIDL 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896334556 256 RLVRGLDYYNRTVFEWVTTSLGAQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ 317
Cdd:cd00773 200 SLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
4.94e-39 |
|
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: 142.34 E-value: 4.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 10 GMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEVTDvvekEMYTFEDRNGESLTLRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 90 RAgIEHGLLYNQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHVKLELNSIG 169
Cdd:pfam13393 77 RI-DAHRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV-PGVTLDLGHVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 170 -------SLEARANYRDALVAFLEQH-----VEVLDEDCKRRMYSNPLRVLDSKNPEVQALLNDAPRLSEYLD-EESRAH 236
Cdd:pfam13393 155 lvralleAAGLSEALEEALRAALQRKdaaelAELAAEAGLPPALRRALLALPDLYGGPEVLDEARAALPGLPAlQEALDE 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896334556 237 FAGLCELLA--QAGIPYTVNERLVRGLDYYNRTVFEWVTtsLGAQGTVCAGGRYDGLVEQLgGRATPAVGFAMGLERL 312
Cdd:pfam13393 235 LEALAALLEalGDGVRLTFDLAELRGYEYYTGIVFAAYA--PGVGEPLARGGRYDDLGAAF-GRARPATGFSLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-424 |
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: 641.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 2 AKNIQAIRGMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEvtDVVEKEMYTFEDRNGESLTLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 82 PEGTAGCVRAGIEHGLLYNQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL-KDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 162 KLELNSIGSLEARAnyrDALVAFLE-----QHVEVLDEDCKRRMYSNPLR-VLDSKNPEVQALLNDAPRLSEYLDEESRA 235
Cdd:COG0124 158 TLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 236 HFAGLCELLAQAGIPYTVNERLVRGLDYYNRTVFEWVTTSLGAQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLL 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 316 VQAVNPEFKAPSAIDVYVISSGAGTQSAAMRLAEQVRDAapQLKLMTNYGGGNFKKQITRADKWGARIALILGESEVAAQ 395
Cdd:COG0124 315 LEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420
....*....|....*....|....*....
gi 896334556 396 QVVVKDLRSGEQETLAQSEVAARLALMLG 424
Cdd:COG0124 393 TVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-412 |
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: 631.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 6 QAIRGMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGESLTLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 86 AGCVRAGIEHGLLYNQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHVKLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL-KDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 166 NSIGSLEARANYRDALVAFLEQHVEVLDEDCKRRMYSNPLRVLDSKNPEVQALLNDAPRLSEYLDEESRAHFAGLCELLA 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 246 QAGIPYTVNERLVRGLDYYNRTVFEWVTTSLGAQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQAVNPEFKA 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 326 PSAIDVYVISSGAGTQSAAMRLAEQVRDAApqLKLMTNYGGGNFKKQITRADKWGARIALILGESEVAAQQVVVKDLRSG 405
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKAG--IRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
gi 896334556 406 EQETLAQ 412
Cdd:TIGR00442 398 EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-414 |
4.85e-148 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 427.39 E-value: 4.85e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 1 MAKnIQAIRGMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGESLTL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 81 RPEGTAGCVRAGIEHGLLY-NQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaE 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQV-K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 160 HVKLELNSIGSLEARANYRDALVAFLEQHVEVLDEDCKRRMYSNPLRVLDSKNPEVQALLNDAPRLSEYLDEESRAHFAG 239
Cdd:CHL00201 159 NLILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 240 LCELLAQAGIPYTVNERLVRGLDYYNRTVFEWVTTSLGAQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ-- 317
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKdn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 318 AVNPEFKapsaIDVYVISSGAGTQSAAMRLAEQVRDAapQLKLMTNYGGGNFKKQITRADKWGARIALILGESEVAAQQV 397
Cdd:CHL00201 319 IILPKQS----IDVYIATQGLKAQKKGWEIIQFLEKQ--NIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCI 392
|
410
....*....|....*..
gi 896334556 398 VVKDLRSGEQETLAQSE 414
Cdd:CHL00201 393 TIKWLDEQVQENAQYSN 409
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-317 |
3.65e-104 |
|
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: 309.15 E-value: 3.65e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 18 ETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRaigEVTDVVEKEMYTFEDRNGESLTLRPEGTAGCVRAGIEHGL 97
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLR---KSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 98 LYNQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHVKLELNSIGSLEARANy 177
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL-KDFQIKINHRGILDGIAG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 178 rdalvafleqhvevldedckrrmysnplrvlDSKNPEVQALlndapRLSEYLDEESRAHFAGLCELLAQAG--IPYTVNE 255
Cdd:cd00773 156 -------------------------------LLEDREEYIE-----RLIDKLDKEALAHLEKLLDYLEALGvdIKYSIDL 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896334556 256 RLVRGLDYYNRTVFEWVTTSLGAQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ 317
Cdd:cd00773 200 SLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
13-317 |
8.26e-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: 165.87 E-value: 8.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 13 DYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEqtplFKRAIGEVTDVVEKEMYTFEDRNGESLTLRPEGTAGCVRAG 92
Cdd:TIGR00443 2 DLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLE----YLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 93 IEHGLLYNQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIAEhVKLEL------- 165
Cdd:TIGR00443 78 STRLRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKD-FKIELghvglvr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 166 ----NSIGSLEARANYRDAL----VAFLEQHVEVLDEDCKR--------RMYSNPLRVLDsknpEVQAlLNDAPRLSEYL 229
Cdd:TIGR00443 157 alleEAGLPEEAREALREALarkdLVALEELVAELGLSPEVrerllalpRLRGDGEEVLE----EARA-LAGSETAEAAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 230 DEESRAHfaglcELLAQAGIP--YTVNERLVRGLDYYNRTVFEWVTTSLGAqgTVCAGGRYDGLVEQLgGRATPAVGFAM 307
Cdd:TIGR00443 232 DELEAVL-----ELLEARGVEeyISLDLGLVRGYHYYTGLIFEGYAPGLGA--PLAGGGRYDELLGRF-GRPLPATGFAL 303
|
330
....*....|
gi 896334556 308 GLERLVLLVQ 317
Cdd:TIGR00443 304 NLERLLEALT 313
|
|
| 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 |
4.73e-44 |
|
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: 153.70 E-value: 4.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 18 ETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIgeVTDVVEKEMYTFEDRNGE----SLTLRPEGTAGCVRAGI 93
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG--HLDGYRKEMYTFEDKGRElrdtDLVLRPAACEPIYQIFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 94 EHGLLY-NQEQRLWYIGPMFRYERPQ---KGRYRQFHQLGAEVFGLQG--PDIDAELILLTARWWKALGiaEHVKLELNS 167
Cdd:cd00670 79 GEILSYrALPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGEPEeaEEERREWLELAEEIARELG--LPVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 168 IGSLEARANyrdalvafleqhvevldedckrrmysnplrvldsknpevqallndaprlseyldeesrahfaglcellaqa 247
Cdd:cd00670 157 DPFFGRGGK----------------------------------------------------------------------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 248 gipytvnerlvRGLDYYNRTVFEWV--TTSLGAQGTVCAGGRYDGLVEQ---------LGGRATPAVGFAMGLERLVLLV 316
Cdd:cd00670 166 -----------RGLDAGRETVVEFEllLPLPGRAKETAVGSANVHLDHFgasfkidedGGGRAHTGCGGAGGEERLVLAL 234
|
.
gi 896334556 317 Q 317
Cdd:cd00670 235 L 235
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
10-354 |
2.46e-42 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 153.48 E-value: 2.46e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 10 GMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGevtDVVEKEMYTFEDR-NGESLTLRPEGTAGC 88
Cdd:PRK12292 8 GIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGG---AILDLRTFKLVDQlSGRTLGLRPDMTAQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 89 VRAgIEHGLLYNQE-QRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHVKLEL-- 165
Cdd:PRK12292 85 ARI-AATRLANRPGpLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGL-PNFTLDLgh 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 166 ---------NSIGSLEARANYRDALVAF----LEQHVEVLDEDCKRRMysnpLRVLDSKNPEvqALLNDAPRLseYLDEE 232
Cdd:PRK12292 163 vglfralleAAGLSEELEEVLRRALANKdyvaLEELVLDLSEELRDAL----LALPRLRGGR--EVLEEARKL--LPSLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 233 SRAHFAGLCELLAQAGiPYTVNERL------VRGLDYYNRTVFEWVTTSLGAQgtVCAGGRYDGLVEQLgGRATPAVGFA 306
Cdd:PRK12292 235 IKRALDELEALAEALE-KYGYGIPLsldlglLRHLDYYTGIVFEGYVDGVGNP--IASGGRYDDLLGRF-GRARPATGFS 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 896334556 307 MGLERLVLLVQAVNPEfkapsAIDVYVISSGAGTQSAAMRLAEQVRDA 354
Cdd:PRK12292 311 LDLDRLLELQLELPVE-----ARKDLVIAPDSEALAAALAAAQELRKK 353
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
9-414 |
2.97e-41 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 152.59 E-value: 2.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 9 RGMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGE-VTDvvekEMYTFEDRNGESLTLRPEGTAG 87
Cdd:PLN02530 74 KGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEeITD----QLYNFEDKGGRRVALRPELTPS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 88 CVRAGIEHGllynQEQRL---WY-IGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGI-AEHVK 162
Cdd:PLN02530 150 LARLVLQKG----KSLSLplkWFaIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGItSSDVG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 163 LELNSIGSLEARANYRDALVAFLEQHVEVLD--EDCKRRMYSNPLRVLDSKNPEVQALLN-----DAPRLSEYLDEESRA 235
Cdd:PLN02530 226 IKVSSRKVLQAVLKSYGIPEESFAPVCVIVDklEKLPREEIEKELDTLGVSEEAIEGILDvlslkSLDDLEALLGADSEA 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 236 hFAGLCEL--LAQAgipYTVNERL------VRGLDYYNRTVFEWVTTSlGAQGTVCAGGRYDGLVEQLGGRATPAVGFAM 307
Cdd:PLN02530 306 -VADLKQLfsLAEA---YGYQDWLvfdasvVRGLAYYTGIVFEGFDRA-GKLRAICGGGRYDRLLSTFGGEDTPACGFGF 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 308 GLERLVLLVQ--AVNPEFkaPSAIDVYVISSGAGTQSAAMRLAEQVRDAAPQLKLMTNygGGNFKKQITRADKWGARIAL 385
Cdd:PLN02530 381 GDAVIVELLKekGLLPEL--PHQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLE--PKKLKWVFKHAERIGAKRLV 456
|
410 420
....*....|....*....|....*....
gi 896334556 386 ILGESEVAAQQVVVKDLRSGEQETLAQSE 414
Cdd:PLN02530 457 LVGASEWERGMVRVKDLSSGEQTEVKLDE 485
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
15-318 |
2.03e-40 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 146.09 E-value: 2.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 15 LPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEVTDvveKEMYTFEDRNGESLTLRPEGTAGCVRAGIE 94
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVARIAAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 95 HglLYNQE--QRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHVKLELNSIG--- 169
Cdd:COG3705 78 R--LANRPgpLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGL-EDFTLDLGHVGlfr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 170 ----SLEARANYRDALVAFLEQ--HVEvLDEDCKRRMYSNPLR--------------VLDsknpEVQALLNDApRLSEYL 229
Cdd:COG3705 155 alleALGLSEEQREELRRALARkdAVE-LEELLAELGLSEELAeallalpelyggeeVLA----RARALLLDA-AIRAAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 230 DEesrahFAGLCELLAQAG--IPYTVNERLVRGLDYYNRTVFEWVTTSLGaqGTVCAGGRYDGLVEQLGgRATPAVGFAM 307
Cdd:COG3705 229 DE-----LEALAEALAARGpdVRLTFDLSELRGYDYYTGIVFEAYAPGVG--DPLARGGRYDGLLAAFG-RARPATGFSL 300
|
330
....*....|.
gi 896334556 308 GLERLVLLVQA 318
Cdd:COG3705 301 DLDRLLRALPA 311
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
4.94e-39 |
|
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: 142.34 E-value: 4.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 10 GMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEVTDvvekEMYTFEDRNGESLTLRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 90 RAgIEHGLLYNQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHVKLELNSIG 169
Cdd:pfam13393 77 RI-DAHRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV-PGVTLDLGHVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 170 -------SLEARANYRDALVAFLEQH-----VEVLDEDCKRRMYSNPLRVLDSKNPEVQALLNDAPRLSEYLD-EESRAH 236
Cdd:pfam13393 155 lvralleAAGLSEALEEALRAALQRKdaaelAELAAEAGLPPALRRALLALPDLYGGPEVLDEARAALPGLPAlQEALDE 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896334556 237 FAGLCELLA--QAGIPYTVNERLVRGLDYYNRTVFEWVTtsLGAQGTVCAGGRYDGLVEQLgGRATPAVGFAMGLERL 312
Cdd:pfam13393 235 LEALAALLEalGDGVRLTFDLAELRGYEYYTGIVFAAYA--PGVGEPLARGGRYDDLGAAF-GRARPATGFSLDLEAL 309
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
6-415 |
4.58e-38 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 142.56 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 6 QAIRGMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLF--KRAIGevtDVVEKEMYTFEDRNGESLTLRPE 83
Cdd:PRK12420 5 RNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMssKYGGG---DEILKEIYTLTDQGKRDLALRYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 84 GTAGCVRAgiehgLLYNQEQRLWY----IGPMFRYERPQKGRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIAe 159
Cdd:PRK12420 82 LTIPFAKV-----VAMNPNIRLPFkryeIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 160 hVKLELNSIGSLearANYRDALVAFLEQHVEV---LD-----------EDCKRRMYSNPL--RVLDSKNPEVQALLND-A 222
Cdd:PRK12420 156 -VTIQYNNRKLL---NGILQAIGIPTELTSDVilsLDkiekigidgvrKDLLERGISEEMadTICNTVLSCLQLSIADfK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 223 PRLSEYLDEESRAHFAGLCELLAQAGIP--YTVNERLVRGLDYYNRTVFEWVTTSLGAQGTVCAGGRYDGLVEQLGG--R 298
Cdd:PRK12420 232 EAFNNPLVAEGVNELQQLQQYLIALGINenCIFNPFLARGLTMYTGTVYEIFLKDGSITSSIGSGGRYDNIIGAFRGddM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 299 ATPAVGFAMGLErlvLLVQAVNPEFKAPSAIDVYVISsgAGTQSAAMRLAEQVRdAAPQLKLMTNYGGGNFKKQITRADK 378
Cdd:PRK12420 312 NYPTVGISFGLD---VIYTALSQKETISSTADVFIIP--LGTELQCLQIAQQLR-STTGLKVELELAGRKLKKALNYANK 385
|
410 420 430
....*....|....*....|....*....|....*..
gi 896334556 379 WGARIALILGESEVAAQQVVVKDLRSGEQETLAQSEV 415
Cdd:PRK12420 386 ENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVPLSSL 422
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
21-173 |
5.01e-34 |
|
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: 126.08 E-value: 5.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 21 LWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEvtdvvEKEMYTFEDRNGESLTLRPEGTAGCVRAGIEHglLYN 100
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE-----PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSH--IRK 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896334556 101 QEQRLWYIGPMFRYERPQKG--RYRQFHQLGAEVFGLQGPD--IDAELILLTARWWKALGIAEHVKLELNSIGSLEA 173
Cdd:cd00768 74 LPLRLAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEasEFEELIELTEELLRALGIKLDIVFVEKTPGEFSP 150
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
68-320 |
7.02e-32 |
|
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: 119.44 E-value: 7.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 68 YTFEDRNGESLTLRPEGTAGCVRAGIEHGL-LYNQEQRLWYIGPMFRYERP--QKG--RYRQFHQLGAEVFGLQG--PDI 140
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLrSKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHAPGqsPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 141 DAELILLTARWWKALGIAEHVKLELNSIGSlearanyrdalvafleqhvevldedckrrmysnplrvldsknpevqalln 220
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGS-------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 221 daprlseyldeesrahfaglcellaqagipytvnerlvrgLDYYNRTVFEWVTTSLGAQG-TVCAGGRYDGLVEQLGGRA 299
Cdd:pfam00587 111 ----------------------------------------AFYGPKLDFEVVFPSLGKQRqTGTIQNDGFRLPRRLGIRY 150
|
250 260 270
....*....|....*....|....*....|.
gi 896334556 300 --------TP-AVGFA-MGLERLVLLVQAVN 320
Cdd:pfam00587 151 kdedneskFPyMIHRAgLGVERFLAAILENN 181
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
328-420 |
5.36e-30 |
|
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: 111.48 E-value: 5.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 328 AIDVYVISSGAGTQSAAMRLAEQVRDAApqLKLMTNYGGGNFKKQITRADKWGARIALILGESEVAAQQVVVKDLRSGEQ 407
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAG--IKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQ 78
|
90
....*....|...
gi 896334556 408 ETLAQSEVAARLA 420
Cdd:cd00859 79 ETVALDELVEELK 91
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
9-423 |
1.76e-28 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 118.07 E-value: 1.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 9 RGMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEVTdvveKEMYTFEDRNGESLTLRPEGTAGC 88
Cdd:PLN02972 331 KGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDS----KLIYDLADQGGELCSLRYDLTVPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 89 VRAGIEHGLlynQEQRLWYIGPMFRYERPQKGRYRQFHQLGAEVFGLQGP-DIDAELI-LLTarwwkalgiaeHVKLELN 166
Cdd:PLN02972 407 ARYVAMNGI---TSFKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPmGPDFEIIkVLT-----------ELLDELD 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 167 sIGSLEARANYRDALVAFLE-------------QHVEVLD----EDCKRRM-----YSNPL-----RVLDSKNPEVQALL 219
Cdd:PLN02972 473 -IGTYEVKLNHRKLLDGMLEicgvppekfrticSSIDKLDkqsfEQVKKEMveekgLSNETadkigNFVKERGPPLELLS 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 220 NDAPRLSEYLDEE-SRA---HFAGLCELLAQAGI--PYTVNERLVRGLDYYNRTVFEWVTtsLGAQ-GTVCAGGRYDGLV 292
Cdd:PLN02972 552 KLRQEGSEFLGNAsSRAaldELEIMFKALEKSKAigKIVFDLSLARGLDYYTGVIYEAVF--KGAQvGSIAAGGRYDNLV 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 293 EQLGGRATPAVGFAMGLERLVLLVQAVNPEFKA---PSAIDVYVISSGAGTQSAAMRLAEQVRDAAPQLKLMTNyggGNF 369
Cdd:PLN02972 630 GMFSGKQVPAVGVSLGIERVFAIMEQQEEEKSQvirPTETEVLVSIIGDDKLALAAELVSELWNAGIKAEYKVS---TRK 706
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 896334556 370 KKQITRADKWGARIALILGESEVAAQQVVVKDLRSGEQETLAQSEVAARLALML 423
Cdd:PLN02972 707 AKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAEL 760
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
65-318 |
2.19e-17 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 83.06 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 65 KEMYTFEDRNGESLTLRPEGTAGCVRAGIEHGLlyNQEQRLWYIGPMFRYerpQKGRYRQFHQLGAEVFGLQGP-DIDAE 143
Cdd:PRK12295 47 RRIFVTSDENGEELCLRPDFTIPVCRRHIATAG--GEPARYAYLGEVFRQ---RRDRASEFLQAGIESFGRADPaAADAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 144 LILLTARWWKALGIAEhVKLELNSIGSLEA--------------------RANYRDALVAFL--------EQHVEVL--- 192
Cdd:PRK12295 122 VLALALEALAALGPGD-LEVRLGDVGLFAAlvdalglppgwkrrllrhfgRPRSLDALLARLagprvdplDEHAGVLaal 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 193 -DEDCKRRMYSNPL------------------RVL--------DSKNPEVQALLNDAPRLSEYLDEESR----------- 234
Cdd:PRK12295 201 aDEAAARALVEDLMsiagispvggrspaeiarRLLekaalaaaARLPAEALAVLERFLAISGPPDAALAalralaadagl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 235 ------AHFAGLCELLAQAGIPYtvnERLV------RGLDYYNRTVFEWVTTSLGAqGTVCAGGRYDGLVEQLG-GRATP 301
Cdd:PRK12295 281 dldaalDRFEARLAALAARGIDL---ERLRfsasfgRPLDYYTGFVFEIRAAGNGD-PPLAGGGRYDGLLTRLGaGEPIP 356
|
330
....*....|....*..
gi 896334556 302 AVGFAMGLERLVLLVQA 318
Cdd:PRK12295 357 AVGFSIWLDRLAALGGA 373
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
330-419 |
4.33e-10 |
|
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: 56.06 E-value: 4.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 330 DVYVISSGAGTQSA---AMRLAEQVRDAapQLKLMTNYGGGNFKKQITRADKWGARIALILGESEVAAQQVVVKDLRSGE 406
Cdd:pfam03129 1 QVVVIPLGEKAEELeeyAQKLAEELRAA--GIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGE 78
|
90
....*....|...
gi 896334556 407 QETLAQSEVAARL 419
Cdd:pfam03129 79 QETVSLDELVEKL 91
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
10-321 |
1.10e-08 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 56.52 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 10 GMNDYLPEETALWQRIEGTLKQVLGGYGYSEIRLPIVEQTPLFKRAIGEVTDVVekemyTFE--DR-NGESLTLRPEGTA 86
Cdd:PRK12421 12 GVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQ-----TFKliDQlSGRLMGVRADITP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 87 GCVRagIEHGLLYNQE-QRLWYIGPMFRyERPQK-GRYRQFHQLGAEVFGLQGPDIDAELILLTARWWKALGIaEHVKLE 164
Cdd:PRK12421 87 QVAR--IDAHLLNREGvARLCYAGSVLH-TLPQGlFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGV-PALHLD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 165 LNSIG---SLEARA----NYRDALVAFLEQH-VEVLDEDCKRRMYSNPLR----VLDSKNPEVQALLNDAPRLSEYlDEE 232
Cdd:PRK12421 163 LGHVGifrRLAELAglspEEEEELFDLLQRKaLPELAEVCQNLGVGSDLRrmfyALARLNGGLEALDRALSVLALQ-DAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 233 SRAHFAGLCELLAQAG-------IPYTVNErlVRGLDYYNRTVFEWVTTSLGAQgtVCAGGRYDGlVEQLGGRATPAVGF 305
Cdd:PRK12421 242 IRQALDELKTLAAHLKnrwpelpVSIDLAE--LRGYHYHTGLVFAAYIPGRGQA--LARGGRYDG-IGEAFGRARPATGF 316
|
330
....*....|....*.
gi 896334556 306 AMGLERLVLLVQAVNP 321
Cdd:PRK12421 317 SMDLKELLALQFLEEE 332
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
14-307 |
9.04e-07 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 49.99 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 14 YLPEETALWQRIEGTLKQVLGGYGYSEIrlpiveQTPLFKRAIGE-VTDvvEKEMYTFEDRNGESLTLRPEGTAGCVRAg 92
Cdd:PRK12293 14 YFGKSAKLKREIENVASEILYENGFEEI------VTPFFSYHQHQsIAD--EKELIRFSDEKNHQISLRADSTLDVVRI- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 93 IEHGLLYNQEQRLW-YIGPMFRYerPQkgryRQFHQLGAEVFGlqGPDIdAELILLTARWWKALGIAEHVKLELNSIGSL 171
Cdd:PRK12293 85 VTKRLGRSTEHKKWfYIQPVFRY--PS----NEIYQIGAELIG--EEDL-SEILNIAAEIFEELELEPILQISNIKIPKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 172 EARaNYRDALVAFLEQHVE-VLDEDCKrrmYSNPLRVLdsKNPE-VQALLNDAP-RLSEYLDEesrahfagLCELLAQAG 248
Cdd:PRK12293 156 VAE-ILGLDIEVFKKGQIEkLLAQNVP---WLNKLVRI--KTLEdLDEVIELVPdEIKEELEK--------LKELAESIK 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 896334556 249 IPYTVNERLVRG-LDYYNRTVFEWvttsLGAQGTVCAGGRY--DGLveqlggratPAVGFAM 307
Cdd:PRK12293 222 YENLVIAPLYYAkMRYYDDLFFRF----FDGNSTLASGGNYeiDGI---------SSSGFAL 270
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
329-419 |
2.81e-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: 45.47 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896334556 329 IDVYVISSGAGTQSA---AMRLAEQVRDAApqLKLMTNYGGGNFKKQITRADKWGARIALILGESEVAAQQVVVKDLRSG 405
Cdd:cd00738 2 IDVAIVPLTDPRVEAreyAQKLLNALLANG--IRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....
gi 896334556 406 EQETLAQSEVAARL 419
Cdd:cd00738 80 ESETLHVDELPEFL 93
|
|
| |
