|
Name |
Accession |
Description |
Interval |
E-value |
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-412 |
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: 626.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 4 QRPKGTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDTTDIVSKEMYDFYDKGERHVTLRPEGT 83
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 84 APIVRSFVEHKLFGPeyaKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQIRL 163
Cdd:TIGR00442 81 APVARAVIENKLLLP---KPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 164 VINSLGDKETRQAYRQALIDYLVPFEEQLSEDSKRRLHENPLRVLDSKDKRDQRFVAEAPSILDFLSESAQKHFDTVVTM 243
Cdd:TIGR00442 158 EINSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 244 LDALDIPYEIDHNMVRGLDYYTHTIFEIMSDapKMGAQATICAGGRYDNLVEELGGPETPGFGFAMGIERLLLTMEAEEV 323
Cdd:TIGR00442 238 LDALGIPYKIDPSLVRGLDYYTGTVFEFVTD--DLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 324 VIPAFNELDAYVVALGEETNIEALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELENQTVTVKAMA 403
Cdd:TIGR00442 316 IPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLE 395
|
....*....
gi 1173275856 404 NRKEKSFPL 412
Cdd:TIGR00442 396 TGEQETVPL 404
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-425 |
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: 601.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 1 MSFQRPKGTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDttDIVSKEMYDFYDKGERHVTLRP 80
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 81 EGTAPIVRSFVEHKLfgpEYAKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQ 160
Cdd:COG0124 80 EGTAPVARAVAEHGN---ELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 161 IRLVINSLGDKETRQayrQALIDYL-----VPFEEQLSEDSKRRLHENPLR-VLDSKDKRDQRFVAEAPSILDFLSESAQ 234
Cdd:COG0124 157 FTLEINSRGLPEERA---EALLRYLdkldkIGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 235 KHFDTVVTMLDALDIPYEIDHNMVRGLDYYTHTIFEIMSDapKMGAQATICAGGRYDNLVEELGGPETPGFGFAMGIERL 314
Cdd:COG0124 234 AHFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTD--GLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 315 LLTMEAEEVVIPAFNELDAYVVALGEETNIEALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELEN 394
Cdd:COG0124 312 LLLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELAN 391
|
410 420 430
....*....|....*....|....*....|.
gi 1173275856 395 QTVTVKAMANRKEKSFPLTEVYEHFDEVYDE 425
Cdd:COG0124 392 GTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-414 |
6.00e-138 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 401.97 E-value: 6.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 1 MSFQRP-KGTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDTTDIVSKEMYDFYDKGERHVTLR 79
Cdd:CHL00201 1 MAKIQAiRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 80 PEGTAPIVRSFVEHKLfgPEYAKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGIN 159
Cdd:CHL00201 81 PEGTAGIVRAFIENKM--DYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 160 QIRLVINSLGDKETRQAYRQALIDYLVPFEEQLSEDSKRRLHENPLRVLDSKDKRDQRFVAEAPSILDFLSESAQKHFDT 239
Cdd:CHL00201 159 NLILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 240 VVTMLDALDIPYEIDHNMVRGLDYYTHTIFEIMSDAPKmgAQATICAGGRYDNLVEELGGPETPGFGFAMGIERLLLTME 319
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSN--GQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 320 aEEVVIPAfNELDAYVVALGEETNIEALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELENQTVTV 399
Cdd:CHL00201 317 -DNIILPK-QSIDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITI 394
|
410
....*....|....*
gi 1173275856 400 KAMANRKEKSFPLTE 414
Cdd:CHL00201 395 KWLDEQVQENAQYSN 409
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
16-319 |
3.71e-98 |
|
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: 294.12 E-value: 3.71e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 16 ESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDttdIVSKEMYDFYDKGERHVTLRPEGTAPIVRSFVEHKL 95
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGD---EVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 96 FGPeyaKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQIRLVINSLG------ 169
Cdd:cd00773 78 SLP---LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGildgia 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 170 -DKETRQAYRQALIDYlvpfeeqlsedskrrlhenplrvldskdkrdqrfvaeapsildfLSESAQKHFDTVVTMLDAL- 247
Cdd:cd00773 155 gLLEDREEYIERLIDK--------------------------------------------LDKEALAHLEKLLDYLEALg 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173275856 248 -DIPYEIDHNMVRGLDYYTHTIFEIMsdAPKMGAQATICAGGRYDNLVEELGGPETPGFGFAMGIERLLLTME 319
Cdd:cd00773 191 vDIKYSIDLSLVRGLDYYTGIVFEAV--ADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-314 |
7.83e-40 |
|
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: 144.65 E-value: 7.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 8 GTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEvisrSVGDTTDIVSKEMYDFYDKGERHVTLRPEGTAPIV 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLD----SLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 88 RSFVeHKLFGPEyakPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQIRLVINS 167
Cdd:pfam13393 77 RIDA-HRLNRPG---PLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 168 LG-----------DKETRQAYRQAL----IDYLVPF--EEQLSEDSKRRLHENP-LRVLDSKDKRDQRFVAEAPSIldfl 229
Cdd:pfam13393 153 VGlvralleaaglSEALEEALRAALqrkdAAELAELaaEAGLPPALRRALLALPdLYGGPEVLDEARAALPGLPAL---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 230 sESAQKHFDTVVTMLDAL--DIPYEIDHNMVRGLDYYTHTIFEIMSDapkmGAQATICAGGRYDNLVEELGGPEtPGFGF 307
Cdd:pfam13393 229 -QEALDELEALAALLEALgdGVRLTFDLAELRGYEYYTGIVFAAYAP----GVGEPLARGGRYDDLGAAFGRAR-PATGF 302
|
....*..
gi 1173275856 308 AMGIERL 314
Cdd:pfam13393 303 SLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-412 |
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: 626.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 4 QRPKGTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDTTDIVSKEMYDFYDKGERHVTLRPEGT 83
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 84 APIVRSFVEHKLFGPeyaKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQIRL 163
Cdd:TIGR00442 81 APVARAVIENKLLLP---KPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 164 VINSLGDKETRQAYRQALIDYLVPFEEQLSEDSKRRLHENPLRVLDSKDKRDQRFVAEAPSILDFLSESAQKHFDTVVTM 243
Cdd:TIGR00442 158 EINSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 244 LDALDIPYEIDHNMVRGLDYYTHTIFEIMSDapKMGAQATICAGGRYDNLVEELGGPETPGFGFAMGIERLLLTMEAEEV 323
Cdd:TIGR00442 238 LDALGIPYKIDPSLVRGLDYYTGTVFEFVTD--DLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 324 VIPAFNELDAYVVALGEETNIEALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELENQTVTVKAMA 403
Cdd:TIGR00442 316 IPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLE 395
|
....*....
gi 1173275856 404 NRKEKSFPL 412
Cdd:TIGR00442 396 TGEQETVPL 404
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-425 |
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: 601.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 1 MSFQRPKGTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDttDIVSKEMYDFYDKGERHVTLRP 80
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 81 EGTAPIVRSFVEHKLfgpEYAKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQ 160
Cdd:COG0124 80 EGTAPVARAVAEHGN---ELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 161 IRLVINSLGDKETRQayrQALIDYL-----VPFEEQLSEDSKRRLHENPLR-VLDSKDKRDQRFVAEAPSILDFLSESAQ 234
Cdd:COG0124 157 FTLEINSRGLPEERA---EALLRYLdkldkIGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 235 KHFDTVVTMLDALDIPYEIDHNMVRGLDYYTHTIFEIMSDapKMGAQATICAGGRYDNLVEELGGPETPGFGFAMGIERL 314
Cdd:COG0124 234 AHFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTD--GLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 315 LLTMEAEEVVIPAFNELDAYVVALGEETNIEALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELEN 394
Cdd:COG0124 312 LLLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELAN 391
|
410 420 430
....*....|....*....|....*....|.
gi 1173275856 395 QTVTVKAMANRKEKSFPLTEVYEHFDEVYDE 425
Cdd:COG0124 392 GTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-414 |
6.00e-138 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 401.97 E-value: 6.00e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 1 MSFQRP-KGTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDTTDIVSKEMYDFYDKGERHVTLR 79
Cdd:CHL00201 1 MAKIQAiRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 80 PEGTAPIVRSFVEHKLfgPEYAKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGIN 159
Cdd:CHL00201 81 PEGTAGIVRAFIENKM--DYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 160 QIRLVINSLGDKETRQAYRQALIDYLVPFEEQLSEDSKRRLHENPLRVLDSKDKRDQRFVAEAPSILDFLSESAQKHFDT 239
Cdd:CHL00201 159 NLILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 240 VVTMLDALDIPYEIDHNMVRGLDYYTHTIFEIMSDAPKmgAQATICAGGRYDNLVEELGGPETPGFGFAMGIERLLLTME 319
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSN--GQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAK 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 320 aEEVVIPAfNELDAYVVALGEETNIEALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELENQTVTV 399
Cdd:CHL00201 317 -DNIILPK-QSIDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITI 394
|
410
....*....|....*
gi 1173275856 400 KAMANRKEKSFPLTE 414
Cdd:CHL00201 395 KWLDEQVQENAQYSN 409
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
16-319 |
3.71e-98 |
|
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: 294.12 E-value: 3.71e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 16 ESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDttdIVSKEMYDFYDKGERHVTLRPEGTAPIVRSFVEHKL 95
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGD---EVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 96 FGPeyaKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQIRLVINSLG------ 169
Cdd:cd00773 78 SLP---LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGildgia 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 170 -DKETRQAYRQALIDYlvpfeeqlsedskrrlhenplrvldskdkrdqrfvaeapsildfLSESAQKHFDTVVTMLDAL- 247
Cdd:cd00773 155 gLLEDREEYIERLIDK--------------------------------------------LDKEALAHLEKLLDYLEALg 190
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1173275856 248 -DIPYEIDHNMVRGLDYYTHTIFEIMsdAPKMGAQATICAGGRYDNLVEELGGPETPGFGFAMGIERLLLTME 319
Cdd:cd00773 191 vDIKYSIDLSLVRGLDYYTGIVFEAV--ADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
11-315 |
8.88e-51 |
|
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: 173.95 E-value: 8.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 11 DILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGdttdIVSKEMYDFYDKGERHVTLRPEGTAPIVRSF 90
Cdd:TIGR00443 2 DLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSG----ILNEDLFKLFDQLGRVLGLRPDMTAPIARLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 91 VEHKlfgPEYAKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQIRLVI----- 165
Cdd:TIGR00443 78 STRL---RDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELghvgl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 166 ------NSLGDKETRQAYRQALIDY-LVPFEE-----QLSEDSKRRLHENPlrvldskdkrdqRFVAEAPSILD-----F 228
Cdd:TIGR00443 155 vralleEAGLPEEAREALREALARKdLVALEElvaelGLSPEVRERLLALP------------RLRGDGEEVLEearalA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 229 LSESAQK---HFDTVVTMLDALDIPYEI--DHNMVRGLDYYTHTIFEIMSDapkmGAQATICAGGRYDNLVEELGGPeTP 303
Cdd:TIGR00443 223 GSETAEAaldELEAVLELLEARGVEEYIslDLGLVRGYHYYTGLIFEGYAP----GLGAPLAGGGRYDELLGRFGRP-LP 297
|
330
....*....|..
gi 1173275856 304 GFGFAMGIERLL 315
Cdd:TIGR00443 298 ATGFALNLERLL 309
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
1-360 |
2.46e-46 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 164.27 E-value: 2.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 1 MSFQRPKGTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDTTDIvskEMYDFYDKGERHVT-LR 79
Cdd:PRK12292 1 MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDL---RTFKLVDQLSGRTLgLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 80 PEGTAPIVRSfVEHKLFGPEYakPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGIN 159
Cdd:PRK12292 78 PDMTAQIARI-AATRLANRPG--PLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 160 QIRLVI-----------NSLGDKETRQAYRQALI--DY--LVPFEEQLSEDSKRRLHE-----NPLRVLDskdkrdqrfv 219
Cdd:PRK12292 155 NFTLDLghvglfralleAAGLSEELEEVLRRALAnkDYvaLEELVLDLSEELRDALLAlprlrGGREVLE---------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 220 aEAPSILdfLSESAQKHFDTVVTMLDALDIPYE-----IDHNMVRGLDYYTHTIFEIMSDapkmGAQATICAGGRYDNLV 294
Cdd:PRK12292 225 -EARKLL--PSLPIKRALDELEALAEALEKYGYgiplsLDLGLLRHLDYYTGIVFEGYVD----GVGNPIASGGRYDDLL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1173275856 295 EELGGPEtPGFGFAMGIERLL-LTMEAEEVVIPAFneldayVVALGEETNIEALKLVQVIRNFGFSA 360
Cdd:PRK12292 298 GRFGRAR-PATGFSLDLDRLLeLQLELPVEARKDL------VIAPDSEALAAALAAAQELRKKGEIV 357
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
1-415 |
3.97e-46 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 164.52 E-value: 3.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 1 MSFQRPKGTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDTTDIVsKEMYDFYDKGERHVTLRP 80
Cdd:PRK12420 2 MEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGDEIL-KEIYTLTDQGKRDLALRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 81 EGTAPIVRSFVehklFGPEYAKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGIN- 159
Cdd:PRK12420 81 DLTIPFAKVVA----MNPNIRLPFKRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLEv 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 160 ----------------------QIRLVINSLgDKETRQAYRQALIDYLvpfEEQLSEDSKRR-----LHENPLRVLDSKD 212
Cdd:PRK12420 157 tiqynnrkllngilqaigipteLTSDVILSL-DKIEKIGIDGVRKDLL---ERGISEEMADTicntvLSCLQLSIADFKE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 213 KRDQRFVAEAPSILDFLSEsaqkhfdtvvtMLDALDIPYEIDHN--MVRGLDYYTHTIFEIMSdapKMGA-QATICAGGR 289
Cdd:PRK12420 233 AFNNPLVAEGVNELQQLQQ-----------YLIALGINENCIFNpfLARGLTMYTGTVYEIFL---KDGSiTSSIGSGGR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 290 YDNLVEELGGPET--PGFGFAMGIERLLLTMEAEEVVIPAfneLDAYVVALGEEtnIEALKLVQVIR-NFGFSADRDFMN 366
Cdd:PRK12420 299 YDNIIGAFRGDDMnyPTVGISFGLDVIYTALSQKETISST---ADVFIIPLGTE--LQCLQIAQQLRsTTGLKVELELAG 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1173275856 367 RKAKAQFKTADKANAKLVLVIGADELENQTVTVKAMANRKEKSFPLTEV 415
Cdd:PRK12420 374 RKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVPLSSL 422
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
6-414 |
5.22e-44 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 160.29 E-value: 5.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 6 PKGTNDILPGES--EKWQFVE--ETARLlfrdYQYNEIRTPIFEHYEVISRSVGDTtdiVSKEMYDFYDKGERHVTLRPE 81
Cdd:PLN02530 73 PKGTRDFPPEDMrlRNWLFDHfrEVSRL----FGFEEVDAPVLESEELYIRKAGEE---ITDQLYNFEDKGGRRVALRPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 82 GTAPIVRSFVEHklfGPEYAKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQ- 160
Cdd:PLN02530 146 LTPSLARLVLQK---GKSLSLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGITSs 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 161 -----------IRLVINSLGDKETRQAYRQALIDYL--VPFEEQLSEDSKRRLHENP----LRVLDSKDKRDQRFV---- 219
Cdd:PLN02530 223 dvgikvssrkvLQAVLKSYGIPEESFAPVCVIVDKLekLPREEIEKELDTLGVSEEAiegiLDVLSLKSLDDLEALlgad 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 220 AEAPSILDFLSESAQK-------HFDTVVtmldaldipyeidhnmVRGLDYYTHTIFEIMSDAPKMGAqatICAGGRYDN 292
Cdd:PLN02530 303 SEAVADLKQLFSLAEAygyqdwlVFDASV----------------VRGLAYYTGIVFEGFDRAGKLRA---ICGGGRYDR 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 293 LVEELGGPETP--GFGF--AMGIERLlltmeAEEVVIPAF-NELDAYVVALGEETNIEALKLVQVIRNFGFSADRDFMNR 367
Cdd:PLN02530 364 LLSTFGGEDTPacGFGFgdAVIVELL-----KEKGLLPELpHQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLEPK 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1173275856 368 KAKAQFKTADKANAKLVLVIGADELENQTVTVKAMANRKEKSFPLTE 414
Cdd:PLN02530 439 KLKWVFKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDE 485
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
13-315 |
5.76e-41 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 147.63 E-value: 5.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 13 LPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDTTDivsKEMYDFYDKGERHVTLRPEGTAPIVRsFVE 92
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVAR-IAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 93 HKLFGPEYakPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQIRLVINSLG--- 169
Cdd:COG3705 77 TRLANRPG--PLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGlfr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 170 --------DKETRQAYRQAL-------IDYLVPfEEQLSEDSKRRLhenpLRVLDSKDKRDQrfVAEAPSILdfLSESAQ 234
Cdd:COG3705 155 allealglSEEQREELRRALarkdaveLEELLA-ELGLSEELAEAL----LALPELYGGEEV--LARARALL--LDAAIR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 235 KHFDTVVTMLDAL-----DIPYEIDHNMVRGLDYYTHTIFEIMSDapkmGAQATICAGGRYDNLVEELGGPEtPGFGFAM 309
Cdd:COG3705 226 AALDELEALAEALaargpDVRLTFDLSELRGYDYYTGIVFEAYAP----GVGDPLARGGRYDGLLAAFGRAR-PATGFSL 300
|
....*.
gi 1173275856 310 GIERLL 315
Cdd:COG3705 301 DLDRLL 306
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-314 |
7.83e-40 |
|
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: 144.65 E-value: 7.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 8 GTNDILPGESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEvisrSVGDTTDIVSKEMYDFYDKGERHVTLRPEGTAPIV 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLD----SLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 88 RSFVeHKLFGPEyakPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMALDFFKQLGINQIRLVINS 167
Cdd:pfam13393 77 RIDA-HRLNRPG---PLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 168 LG-----------DKETRQAYRQAL----IDYLVPF--EEQLSEDSKRRLHENP-LRVLDSKDKRDQRFVAEAPSIldfl 229
Cdd:pfam13393 153 VGlvralleaaglSEALEEALRAALqrkdAAELAELaaEAGLPPALRRALLALPdLYGGPEVLDEARAALPGLPAL---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 230 sESAQKHFDTVVTMLDAL--DIPYEIDHNMVRGLDYYTHTIFEIMSDapkmGAQATICAGGRYDNLVEELGGPEtPGFGF 307
Cdd:pfam13393 229 -QEALDELEALAALLEALgdGVRLTFDLAELRGYEYYTGIVFAAYAP----GVGEPLARGGRYDDLGAAFGRAR-PATGF 302
|
....*..
gi 1173275856 308 AMGIERL 314
Cdd:pfam13393 303 SLDLEAL 309
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
6-423 |
2.30e-32 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 130.01 E-value: 2.30e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 6 PKGTNDILPgesEKWQFVEETARLL---FRDYQYNEIRTPIFEHYEVISRSVGDTtdivSKEMYDFYDKGERHVTLRPEG 82
Cdd:PLN02972 330 PKGTRDFAK---EQMAIREKAFSIItsvFKRHGATALDTPVFELRETLMGKYGED----SKLIYDLADQGGELCSLRYDL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 83 TAPIVRSFVEHKLfgpeyaKPYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENP-ATDVESMVMALDFFKQLGINQI 161
Cdd:PLN02972 403 TVPFARYVAMNGI------TSFKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPmGPDFEIIKVLTELLDELDIGTY 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 162 RLVINSLG--------------------------DKETRQAYRQALIDylvpfEEQLSEDSKRRLHE------NPLRVLD 209
Cdd:PLN02972 477 EVKLNHRKlldgmleicgvppekfrticssidklDKQSFEQVKKEMVE-----EKGLSNETADKIGNfvkergPPLELLS 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 210 SKDKRDQRFVAeapsildflSESAQKHFDTVVTMLDALDIPYEI-----DHNMVRGLDYYTHTIFEimsdAPKMGAQ-AT 283
Cdd:PLN02972 552 KLRQEGSEFLG---------NASSRAALDELEIMFKALEKSKAIgkivfDLSLARGLDYYTGVIYE----AVFKGAQvGS 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 284 ICAGGRYDNLVEELGGPETPGFGFAMGIERLLLTME-----AEEVVIPAfnELDAYVVALGEETNIEALKLVQVIRNFGF 358
Cdd:PLN02972 619 IAAGGRYDNLVGMFSGKQVPAVGVSLGIERVFAIMEqqeeeKSQVIRPT--ETEVLVSIIGDDKLALAAELVSELWNAGI 696
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1173275856 359 SADRDFMNRKAKaQFKTADKANAKLVLVIGADELENQTVTVKAMANRKEKSFPLTEVYEHFDEVY 423
Cdd:PLN02972 697 KAEYKVSTRKAK-HLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAEL 760
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
330-419 |
7.73e-24 |
|
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: 94.53 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 330 ELDAYVVALGEETNIEALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELENQTVTVKAMANRKEKS 409
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQET 80
|
90
....*....|
gi 1173275856 410 FPLTEVYEHF 419
Cdd:cd00859 81 VALDELVEEL 90
|
|
| 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 ... |
16-186 |
2.02e-23 |
|
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: 97.85 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 16 ESEKWQFVEETARLLFRDYQYNEIRTPIFEHYEVISRsvGDTTDIVSKEMYDFYDKGE----RHVTLRPEGTAPIVRSFV 91
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFK--GGHLDGYRKEMYTFEDKGRelrdTDLVLRPAACEPIYQIFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 92 EHKLfgPEYAKPYKTFYMGPMFRYERPQ---KGRLRQFHQIGVEAFG--SENPATDVESMVMALDFFKQLGINqIRLVIN 166
Cdd:cd00670 79 GEIL--SYRALPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGepEEAEEERREWLELAEEIARELGLP-VRVVVA 155
|
170 180
....*....|....*....|....*
gi 1173275856 167 SLGD-----KETRQAYRQALIDYLV 186
Cdd:cd00670 156 DDPFfgrggKRGLDAGRETVVEFEL 180
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
78-315 |
5.12e-16 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 79.21 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 78 LRPEGTAPIVRSFVEHKLfgpeyAKPYKTFYMGPMFRYerpQKGRLRQFHQIGVEAFGSENP-ATDVESMVMALDFFKQL 156
Cdd:PRK12295 62 LRPDFTIPVCRRHIATAG-----GEPARYAYLGEVFRQ---RRDRASEFLQAGIESFGRADPaAADAEVLALALEALAAL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 157 GINQIRL----------VINSLGDKETRQA----------YRQALIDYLV-----PFEE--------------------- 190
Cdd:PRK12295 134 GPGDLEVrlgdvglfaaLVDALGLPPGWKRrllrhfgrprSLDALLARLAgprvdPLDEhagvlaaladeaaaralvedl 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 191 ----QLSEDSKRRLHENPLRVLD-SKDKRDQRFVAEAPSILD-FLS-----------------------ESAQKHFDTVV 241
Cdd:PRK12295 214 msiaGISPVGGRSPAEIARRLLEkAALAAAARLPAEALAVLErFLAisgppdaalaalralaadagldlDAALDRFEARL 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1173275856 242 TMLDALDIPYE---IDHNMVRGLDYYTHTIFEIMSDAPKMgaqATICAGGRYDNLVEELGGPE-TPGFGFAMGIERLL 315
Cdd:PRK12295 294 AALAARGIDLErlrFSASFGRPLDYYTGFVFEIRAAGNGD---PPLAGGGRYDGLLTRLGAGEpIPAVGFSIWLDRLA 368
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
20-212 |
1.30e-14 |
|
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: 72.54 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 20 WQFVEETARLLFRDYQYNEIRTPIFEHyevisRSVGDTTDIVSKEMYDFYDKGERHVTLRPEGTAPIVRSFVEHKLFGPE 99
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVER-----EPLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 100 yakpyKTFYMGPMFRYERPQKG--RLRQFHQIGVEAFGSENP-ATDVESMVMAL-DFFKQLGIN-QIRLVINSLGDKETR 174
Cdd:cd00768 77 -----RLAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEeASEFEELIELTeELLRALGIKlDIVFVEKTPGEFSPG 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 1173275856 175 QAYRQALIDYLVPFEEQLSEDSKRRLHENPLRVLDSKD 212
Cdd:cd00768 152 GAGPGFEIEVDHPEGRGLEIGSGGYRQDEQARAADLYF 189
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
66-191 |
1.71e-12 |
|
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: 65.51 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 66 YDFYDKGERHVTLRPEGTAPIVRSFVEHKLfgPEYAKPYKTFYMGPMFRYERP--QKG--RLRQFHQIGVEAFGSENPAT 141
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGL--RSKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHAPGQSP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1173275856 142 D-VESMVMALD-FFKQLGInQIRLVINSLGDKETRQAYRqalIDYLVPFEEQ 191
Cdd:pfam00587 79 DeLEDYIKLIDrVYSRLGL-EVRVVRLSNSDGSAFYGPK---LDFEVVFPSL 126
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
332-417 |
1.46e-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: 57.60 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 332 DAYVVALGEETNI---EALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELENQTVTVKAMANRKEK 408
Cdd:pfam03129 1 QVVVIPLGEKAEEleeYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
....*....
gi 1173275856 409 SFPLTEVYE 417
Cdd:pfam03129 81 TVSLDELVE 89
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
23-158 |
2.33e-08 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 55.00 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 23 VEETARLLFRDYQYNEIRTPIFEHYEviSRSVGDttdivSKEMYDFYDKGERHVTLRPEGTAPIVRsFVEHKLFGPEYAK 102
Cdd:PRK12293 25 IENVASEILYENGFEEIVTPFFSYHQ--HQSIAD-----EKELIRFSDEKNHQISLRADSTLDVVR-IVTKRLGRSTEHK 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1173275856 103 pyKTFYMGPMFRYerPQkgrlRQFHQIGVEAFGSENPAtdvESMVMALDFFKQLGI 158
Cdd:PRK12293 97 --KWFYIQPVFRY--PS----NEIYQIGAELIGEEDLS---EILNIAAEIFEELEL 141
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
331-419 |
9.21e-08 |
|
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: 49.70 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 331 LDAYVVALGE---ETNIEALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELENQTVTVKAMANRKE 407
Cdd:cd00738 2 IDVAIVPLTDprvEAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGES 81
|
90
....*....|..
gi 1173275856 408 KSFPLTEVYEHF 419
Cdd:cd00738 82 ETLHVDELPEFL 93
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
323-419 |
3.70e-07 |
|
ThrRS Threonyl-anticodon binding domain. ThrRS 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: 238437 [Multi-domain] Cd Length: 91 Bit Score: 47.88 E-value: 3.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 323 VVIPAFNELDAYvvalgeetnieALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELENQTVTVKAM 402
Cdd:cd00860 5 VVIPVTDEHLDY-----------AKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTR 73
|
90
....*....|....*..
gi 1173275856 403 ANRKEKSFPLTEVYEHF 419
Cdd:cd00860 74 DGGDLGSMSLDEFIEKL 90
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
333-421 |
1.74e-04 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 43.99 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 333 AYVVALGEETNIEALKLVQVIRNFGFSADRDFMNRKAKAQFKTADKANAKLVLVIGADELENQTVTVKAMANRKEKSFPL 412
Cdd:PLN02908 592 AIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKI 671
|
....*....
gi 1173275856 413 TEVYEHFDE 421
Cdd:PLN02908 672 EELLTEFKE 680
|
|
| pylS |
PRK09537 |
pyrrolysine--tRNA(Pyl) ligase; |
23-159 |
1.63e-03 |
|
pyrrolysine--tRNA(Pyl) ligase;
Pssm-ID: 236555 [Multi-domain] Cd Length: 417 Bit Score: 40.59 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173275856 23 VEETARLLFRDYQYNEIRTPIFEHYEVISRSVGDTTDIVSKEMYdfydKGERHVTLRPEgTAPIVRSFVehKLFGPEYAK 102
Cdd:PRK09537 209 LERDITKFFVDRGFLEIKSPILIPAEYIERMGIDNDTELSKQIF----RVDKNFCLRPM-LAPGLYNYL--RKLDRILPD 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1173275856 103 PYKTFYMGPMFRYERPQKGRLRQFHQIGVEAFGSENPATDVESMVMalDFFKQLGIN 159
Cdd:PRK09537 282 PIKIFEIGPCYRKESDGKEHLEEFTMVNFCQMGSGCTRENLENIID--DFLKHLGID 336
|
|
| |
