|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-426 |
1.77e-162 |
|
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: 463.82 E-value: 1.77e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 1 MEFNKPRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGI-KEEIYHFQDKGGRDLALRPEL 79
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIvEKEMYTFEDRGGRSLTLRPEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 80 TASVSRLYNNNLQKSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINI 159
Cdd:COG0124 82 TAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDFTLEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 160 GHLGiikgvlnqlnISSQQQTAIIASIDKEDYELLDKLLEDNDISSEYKNIITSIINIKGS--RSDLETLKQLLEDIPEs 237
Cdd:COG0124 162 NSRG----------LPEERAEALLRYLDKLDKIGHEDVLDEDSQRRLETNPLRAILDSKGPdcQEVLADAPKLLDYLGE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 238 fEALENLDKTLEVLEVFGFdDYVVNLSIARGLDYYTGIVFEIYVPDLGAEKQITGGGTY-NLTALFDSEKVESTGFAFGF 316
Cdd:COG0124 231 -EGLAHFEEVLELLDALGI-PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYdGLVEQLGGPPTPAVGFAIGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 317 DRIMEAYHRQNIQVPISSKPKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMIGQQE 396
Cdd:COG0124 309 ERLLLLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDE 388
|
410 420 430
....*....|....*....|....*....|
gi 499725512 397 VEDETVTIKDMDSGCQETIPQNTVVSELLK 426
Cdd:COG0124 389 LANGTVTLKDLATGEQETVPLDELVEYLKE 418
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-417 |
1.10e-158 |
|
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: 453.47 E-value: 1.10e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 4 NKPRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEG---IKEEIYHFQDKGGRDLALRPELT 80
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEEtdiVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 81 ASVSRLYNNNLQKSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINIG 160
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTLEIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 161 HLGIIKGVLNqlnissqQQTAIIASIDKEdyelLDKLLED--NDISSEYKNIITSIInikgsrsdlETLKQLLEDIPESF 238
Cdd:TIGR00442 161 SLGILEGRLE-------YREALIRYLDKH----KDKLGEDsvRRLEKNPLRILDSKN---------EKIQELLKNAPKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 239 -----EALENLDKTLEVLEVFGFdDYVVNLSIARGLDYYTGIVFEIYVPDLGAEKQITGGGTY-NLTALFDSEKVESTGF 312
Cdd:TIGR00442 221 dflceESRAHFEELKELLDALGI-PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYdGLVEELGGPPTPAVGF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 313 AFGFDRIMEAYHRQNIQVPISSKPKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMI 392
Cdd:TIGR00442 300 AIGIERLILLLEELGLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALII 379
|
410 420
....*....|....*....|....*
gi 499725512 393 GQQEVEDETVTIKDMDSGCQETIPQ 417
Cdd:TIGR00442 380 GEDELENGTVTLKDLETGEQETVPL 404
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
16-322 |
9.02e-103 |
|
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: 305.68 E-value: 9.02e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 16 DMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIKEEIYHFQDKGGRDLALRPELTASVSRLYNNNLQKSA 95
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 96 KPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINIGHLGIIKGVLNQLNIS 175
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAGLLEDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 176 SQQQTAIIasidkedyELLDKlledndisseykniitsiinikgsrsdletlkqlledipesfEALENLDKTLEVLEVFG 255
Cdd:cd00773 161 EEYIERLI--------DKLDK------------------------------------------EALAHLEKLLDYLEALG 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499725512 256 FDD-YVVNLSIARGLDYYTGIVFEIYVPDLGAEKQITGGGTY-NLTALFDSEKVESTGFAFGFDRIMEA 322
Cdd:cd00773 191 VDIkYSIDLSLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYdGLLEEFGGEDVPAVGFAIGLERLLLA 259
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
1-381 |
1.56e-77 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 245.55 E-value: 1.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 1 MEFNKPRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIKEEIYHFQDKG-GRDLALRPEL 79
Cdd:PRK12292 1 MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLRTFKLVDQLsGRTLGLRPDM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 80 TASVSRLYNNNLQKSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINI 159
Cdd:PRK12292 81 TAQIARIAATRLANRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 160 GHLGIIKGVLNQLNISSQQQTAIIASIDKEDYELLDKLLEdnDISSEYKNIITSIINIKGSRSDLETLKQLLEDiPESFE 239
Cdd:PRK12292 161 GHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEELVL--DLSEELRDALLALPRLRGGREVLEEARKLLPS-LPIKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 240 ALENLDKTLEVLEVFGFDDYV-VNLSIARGLDYYTGIVFEIYVPDLGAEkqITGGGTY-NLTALFdSEKVESTGFAFGFD 317
Cdd:PRK12292 238 ALDELEALAEALEKYGYGIPLsLDLGLLRHLDYYTGIVFEGYVDGVGNP--IASGGRYdDLLGRF-GRARPATGFSLDLD 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499725512 318 RIMEAYHRQNIQvpissKPKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYA 381
Cdd:PRK12292 315 RLLELQLELPVE-----ARKDLVIAPDSEALAAALAAAQELRKKGEIVVLALPGRNFEDAREYA 373
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-319 |
6.13e-59 |
|
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: 194.73 E-value: 6.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 8 GTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIkEEIYHFQDKGGRDLALRPELTASVSRLY 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADL-DQTFKLVDQSGRLLGLRADITPQVARID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 88 NNNLQKSAkPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINIGHLGIIKG 167
Cdd:pfam13393 80 AHRLNRPG-PLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 168 VLNQLNISSQQQTAIIASIDKEDYELLDKLLEDNDISSEYKNIITSIINIKGSRSDLETLKQLLEDIPESFEALENLDKT 247
Cdd:pfam13393 159 LLEAAGLSEALEEALRAALQRKDAAELAELAAEAGLPPALRRALLALPDLYGGPEVLDEARAALPGLPALQEALDELEAL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499725512 248 LEVLEVFGFD-DYVVNLSIARGLDYYTGIVFEIYVPDLGAEkqITGGGTY-NLTALFDSEKvESTGFAFGFDRI 319
Cdd:pfam13393 239 AALLEALGDGvRLTFDLAELRGYEYYTGIVFAAYAPGVGEP--LARGGRYdDLGAAFGRAR-PATGFSLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-426 |
1.77e-162 |
|
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: 463.82 E-value: 1.77e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 1 MEFNKPRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGI-KEEIYHFQDKGGRDLALRPEL 79
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIvEKEMYTFEDRGGRSLTLRPEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 80 TASVSRLYNNNLQKSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINI 159
Cdd:COG0124 82 TAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDFTLEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 160 GHLGiikgvlnqlnISSQQQTAIIASIDKEDYELLDKLLEDNDISSEYKNIITSIINIKGS--RSDLETLKQLLEDIPEs 237
Cdd:COG0124 162 NSRG----------LPEERAEALLRYLDKLDKIGHEDVLDEDSQRRLETNPLRAILDSKGPdcQEVLADAPKLLDYLGE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 238 fEALENLDKTLEVLEVFGFdDYVVNLSIARGLDYYTGIVFEIYVPDLGAEKQITGGGTY-NLTALFDSEKVESTGFAFGF 316
Cdd:COG0124 231 -EGLAHFEEVLELLDALGI-PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYdGLVEQLGGPPTPAVGFAIGL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 317 DRIMEAYHRQNIQVPISSKPKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMIGQQE 396
Cdd:COG0124 309 ERLLLLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDE 388
|
410 420 430
....*....|....*....|....*....|
gi 499725512 397 VEDETVTIKDMDSGCQETIPQNTVVSELLK 426
Cdd:COG0124 389 LANGTVTLKDLATGEQETVPLDELVEYLKE 418
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-417 |
1.10e-158 |
|
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: 453.47 E-value: 1.10e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 4 NKPRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEG---IKEEIYHFQDKGGRDLALRPELT 80
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEEtdiVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 81 ASVSRLYNNNLQKSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINIG 160
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTLEIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 161 HLGIIKGVLNqlnissqQQTAIIASIDKEdyelLDKLLED--NDISSEYKNIITSIInikgsrsdlETLKQLLEDIPESF 238
Cdd:TIGR00442 161 SLGILEGRLE-------YREALIRYLDKH----KDKLGEDsvRRLEKNPLRILDSKN---------EKIQELLKNAPKIL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 239 -----EALENLDKTLEVLEVFGFdDYVVNLSIARGLDYYTGIVFEIYVPDLGAEKQITGGGTY-NLTALFDSEKVESTGF 312
Cdd:TIGR00442 221 dflceESRAHFEELKELLDALGI-PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYdGLVEELGGPPTPAVGF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 313 AFGFDRIMEAYHRQNIQVPISSKPKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMI 392
Cdd:TIGR00442 300 AIGIERLILLLEELGLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALII 379
|
410 420
....*....|....*....|....*
gi 499725512 393 GQQEVEDETVTIKDMDSGCQETIPQ 417
Cdd:TIGR00442 380 GEDELENGTVTLKDLETGEQETVPL 404
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
16-322 |
9.02e-103 |
|
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: 305.68 E-value: 9.02e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 16 DMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIKEEIYHFQDKGGRDLALRPELTASVSRLYNNNLQKSA 95
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 96 KPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINIGHLGIIKGVLNQLNIS 175
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAGLLEDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 176 SQQQTAIIasidkedyELLDKlledndisseykniitsiinikgsrsdletlkqlledipesfEALENLDKTLEVLEVFG 255
Cdd:cd00773 161 EEYIERLI--------DKLDK------------------------------------------EALAHLEKLLDYLEALG 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499725512 256 FDD-YVVNLSIARGLDYYTGIVFEIYVPDLGAEKQITGGGTY-NLTALFDSEKVESTGFAFGFDRIMEA 322
Cdd:cd00773 191 VDIkYSIDLSLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYdGLLEEFGGEDVPAVGFAIGLERLLLA 259
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
13-326 |
7.48e-86 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 264.35 E-value: 7.48e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 13 LFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIKEEIYHFQDKGGRDLALRPELTASVSRLYNNNLQ 92
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLQTFKLVDQLGRTLGLRPDMTPQVARIAATRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 93 KSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINIGHLGIIKGVLNQL 172
Cdd:COG3705 81 NRPGPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 173 NISSQQQTAIIASIDKEDYELLDKLLEDNDISSEYKNIITSIINIKGSRSDLETLKQLLEDiPESFEALENLDKTLEVLE 252
Cdd:COG3705 161 GLSEEQREELRRALARKDAVELEELLAELGLSEELAEALLALPELYGGEEVLARARALLLD-AAIRAALDELEALAEALA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499725512 253 VFGFDDYV-VNLSIARGLDYYTGIVFEIYVPDLGAEkqITGGGTY-NLTALFDSEkVESTGFAFGFDRIMEAYHRQ 326
Cdd:COG3705 240 ARGPDVRLtFDLSELRGYDYYTGIVFEAYAPGVGDP--LARGGRYdGLLAAFGRA-RPATGFSLDLDRLLRALPAA 312
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
10-322 |
4.28e-84 |
|
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: 259.85 E-value: 4.28e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 10 RDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGiKEEIYHFQDKGGRDLALRPELTASVSRLYNN 89
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGIL-NEDLFKLFDQLGRVLGLRPDMTAPIARLVST 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 90 NLQKSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINIGHLGIIKGVL 169
Cdd:TIGR00443 80 RLRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 170 NQLNISSQQQTAIIASIDKEDYELLDKLLEDNDISSEYKNIITSIINIKGSRSD-LETLKQLLEDiPESFEALENLDKTL 248
Cdd:TIGR00443 160 EEAGLPEEAREALREALARKDLVALEELVAELGLSPEVRERLLALPRLRGDGEEvLEEARALAGS-ETAEAALDELEAVL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499725512 249 EVLEVFGFDDYV-VNLSIARGLDYYTGIVFEIYVPDLGAekQITGGGTY-NLTALFdSEKVESTGFAFGFDRIMEA 322
Cdd:TIGR00443 239 ELLEARGVEEYIsLDLGLVRGYHYYTGLIFEGYAPGLGA--PLAGGGRYdELLGRF-GRPLPATGFALNLERLLEA 311
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
1-381 |
1.56e-77 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 245.55 E-value: 1.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 1 MEFNKPRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIKEEIYHFQDKG-GRDLALRPEL 79
Cdd:PRK12292 1 MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLRTFKLVDQLsGRTLGLRPDM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 80 TASVSRLYNNNLQKSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINI 159
Cdd:PRK12292 81 TAQIARIAATRLANRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 160 GHLGIIKGVLNQLNISSQQQTAIIASIDKEDYELLDKLLEdnDISSEYKNIITSIINIKGSRSDLETLKQLLEDiPESFE 239
Cdd:PRK12292 161 GHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEELVL--DLSEELRDALLALPRLRGGREVLEEARKLLPS-LPIKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 240 ALENLDKTLEVLEVFGFDDYV-VNLSIARGLDYYTGIVFEIYVPDLGAEkqITGGGTY-NLTALFdSEKVESTGFAFGFD 317
Cdd:PRK12292 238 ALDELEALAEALEKYGYGIPLsLDLGLLRHLDYYTGIVFEGYVDGVGNP--IASGGRYdDLLGRF-GRARPATGFSLDLD 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499725512 318 RIMEAYHRQNIQvpissKPKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYA 381
Cdd:PRK12292 315 RLLELQLELPVE-----ARKDLVIAPDSEALAAALAAAQELRKKGEIVVLALPGRNFEDAREYA 373
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
1-415 |
2.94e-70 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 229.63 E-value: 2.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 1 MEFNKPRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIKEEIYHFQDKGGRDLALRPELT 80
Cdd:PLN02530 68 IDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEITDQLYNFEDKGGRRVALRPELT 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 81 ASVSRLYNNNLQKSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINI- 159
Cdd:PLN02530 148 PSLARLVLQKGKSLSLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGITSSDVGIk 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 160 -GHLGIIKGVLNQLNISSQQQTA---IIASIDKEDYELLDKLLEDNDISSEYKNIITSIINIKgSRSDLETLkqlledIP 235
Cdd:PLN02530 228 vSSRKVLQAVLKSYGIPEESFAPvcvIVDKLEKLPREEIEKELDTLGVSEEAIEGILDVLSLK-SLDDLEAL------LG 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 236 ESFEALENLDKTLEVLEVFGFDDYVV-NLSIARGLDYYTGIVFEIYVPDlGAEKQITGGGTYN-LTALFDSEKVESTGFA 313
Cdd:PLN02530 301 ADSEAVADLKQLFSLAEAYGYQDWLVfDASVVRGLAYYTGIVFEGFDRA-GKLRAICGGGRYDrLLSTFGGEDTPACGFG 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 314 FGFDRIMEAYHRQNIQVPISSKPKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMIG 393
Cdd:PLN02530 380 FGDAVIVELLKEKGLLPELPHQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLEPKKLKWVFKHAERIGAKRLVLVG 459
|
410 420
....*....|....*....|..
gi 499725512 394 QQEVEDETVTIKDMDSGCQETI 415
Cdd:PLN02530 460 ASEWERGMVRVKDLSSGEQTEV 481
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
1-416 |
1.87e-65 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 215.37 E-value: 1.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 1 MEFNKPRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEG--IKEEIYHFQDKGGRDLALRPE 78
Cdd:PRK12420 2 MEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGdeILKEIYTLTDQGKRDLALRYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 79 LTASVSRL--YNNNLQKsakPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYe 156
Cdd:PRK12420 82 LTIPFAKVvaMNPNIRL---PFKRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLEVT- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 157 INIGHLGIIKGVLNQLNISSQQQTAIIASIDKEDY----ELLDKLLEDNdISSEYKNIITSIINIkGSRSDLETLKQLLE 232
Cdd:PRK12420 158 IQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKigidGVRKDLLERG-ISEEMADTICNTVLS-CLQLSIADFKEAFN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 233 DiPESFEALENLDKTLEVLEVFGFDDYVV-NLSIARGLDYYTGIVFEIYVPDLGAEKQITGGGTYN--LTALFDSEK-VE 308
Cdd:PRK12420 236 N-PLVAEGVNELQQLQQYLIALGINENCIfNPFLARGLTMYTGTVYEIFLKDGSITSSIGSGGRYDniIGAFRGDDMnYP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 309 STGFAFGFDRIMEAYHRQNIqvpISSKPKVLVIPVKKEfkLNAIEVAQQLRAHN-IVTDIDLKGKKLKKNLSYANNHNFN 387
Cdd:PRK12420 315 TVGISFGLDVIYTALSQKET---ISSTADVFIIPLGTE--LQCLQIAQQLRSTTgLKVELELAGRKLKKALNYANKENIP 389
|
410 420
....*....|....*....|....*....
gi 499725512 388 KVIMIGQQEVEDETVTIKDMDSGCQETIP 416
Cdd:PRK12420 390 YVLIIGEEEVSTGTVMLRNMKEGSEVKVP 418
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-319 |
6.13e-59 |
|
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: 194.73 E-value: 6.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 8 GTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIkEEIYHFQDKGGRDLALRPELTASVSRLY 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADL-DQTFKLVDQSGRLLGLRADITPQVARID 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 88 NNNLQKSAkPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINIGHLGIIKG 167
Cdd:pfam13393 80 AHRLNRPG-PLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVRA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 168 VLNQLNISSQQQTAIIASIDKEDYELLDKLLEDNDISSEYKNIITSIINIKGSRSDLETLKQLLEDIPESFEALENLDKT 247
Cdd:pfam13393 159 LLEAAGLSEALEEALRAALQRKDAAELAELAAEAGLPPALRRALLALPDLYGGPEVLDEARAALPGLPALQEALDELEAL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499725512 248 LEVLEVFGFD-DYVVNLSIARGLDYYTGIVFEIYVPDLGAEkqITGGGTY-NLTALFDSEKvESTGFAFGFDRI 319
Cdd:pfam13393 239 AALLEALGDGvRLTFDLAELRGYEYYTGIVFAAYAPGVGEP--LARGGRYdDLGAAFGRAR-PATGFSLDLEAL 309
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
6-424 |
2.98e-53 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 189.71 E-value: 2.98e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 6 PRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIKeEIYHFQDKGGRDLALRPELTASVSR 85
Cdd:PLN02972 330 PKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSK-LIYDLADQGGELCSLRYDLTVPFAR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 86 LYNNNlqkSAKPLKMYYFGSCFRYERPQAGRFREFWQFGIEVIGGV-PIYNEAEIIAMANEALTQVGIKNYEINIGHLGI 164
Cdd:PLN02972 409 YVAMN---GITSFKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYePMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 165 IKGVLNQLNISSQQQTAIIASIDKED---YELLDK-LLEDNDISSEYKNIITSIINIKGsrSDLETLKQLLE------DI 234
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDkqsFEQVKKeMVEEKGLSNETADKIGNFVKERG--PPLELLSKLRQegseflGN 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 235 PESFEALENLDKTLEVLEVFG-FDDYVVNLSIARGLDYYTGIVFEIYVpdLGAE-KQITGGGTY-NLTALFDSEKVESTG 311
Cdd:PLN02972 564 ASSRAALDELEIMFKALEKSKaIGKIVFDLSLARGLDYYTGVIYEAVF--KGAQvGSIAAGGRYdNLVGMFSGKQVPAVG 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 312 FAFGFDR---IMEAYHRQNIQVPISSKPKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIdLKGKKLKKNLSYANNHNFNK 388
Cdd:PLN02972 642 VSLGIERvfaIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAEY-KVSTRKAKHLKRAKESGIPW 720
|
410 420 430
....*....|....*....|....*....|....*.
gi 499725512 389 VIMIGQQEVEDETVTIKDMDSGCQETIPQNTVVSEL 424
Cdd:PLN02972 721 MVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQEL 756
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
7-415 |
9.33e-53 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 182.41 E-value: 9.33e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 7 RGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEG---IKEEIYHFQDKGGRDLALRPELTASV 83
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETtdiVNKEMYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 84 SR-------LYNNNLQKsakplkMYYFGSCFRYERPQAGRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYE 156
Cdd:CHL00201 88 VRafienkmDYHSNLQR------LWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKNLI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 157 INIGHLGIIKgvlnqlnissqqqtaiiasiDKEDYEL-LDKLLED--NDISSEYKNIITS----IINIKGSRSdletlKQ 229
Cdd:CHL00201 162 LDINSIGKLE--------------------DRQSYQLkLVEYLSQyqDDLDTDSQNRLYSnpirILDSKNLKT-----QE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 230 LLEDIPE-----SFEALENLDKTLEVLEVFGFdDYVVNLSIARGLDYYTGIVFEIYVPDLGAEKQITGGGTYN-LTALFD 303
Cdd:CHL00201 217 ILDGAPKisdflSLESTEHFYDVCTYLNLLNI-PYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDsLIHQLG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 304 SEKVESTGFAFGFDRIMEAYhRQNIQVPissKPKVLVIPVKKEFKLN--AIEVAQQLRAHNIVTDIDLKGKKLKKNLSYA 381
Cdd:CHL00201 296 GPKTPAVGCAIGLERLLLIA-KDNIILP---KQSIDVYIATQGLKAQkkGWEIIQFLEKQNIKFELDLSSSNFHKQIKQA 371
|
410 420 430
....*....|....*....|....*....|....
gi 499725512 382 NNHNFNKVIMIGQQEVEDETVTIKDMDSGCQETI 415
Cdd:CHL00201 372 GKKRAKACIILGDNEIMDNCITIKWLDEQVQENA 405
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
35-319 |
2.01e-30 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 120.42 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 35 GFKEIKTPIFEDLELFTTKSGEGIKEEIYHFQDKGGRDLALRPELTASVSRLYNNNlqKSAKPLKMYYFGSCFRYerpQA 114
Cdd:PRK12295 22 GAVRVDPPILQPAEPFLDLSGEDIRRRIFVTSDENGEELCLRPDFTIPVCRRHIAT--AGGEPARYAYLGEVFRQ---RR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 115 GRFREFWQFGIEVIGGV-PIYNEAEIIAMANEALTQVGIKNYEINIGHLGIIKGVLNQLNISSQQQTAIIASIDKEDY-- 191
Cdd:PRK12295 97 DRASEFLQAGIESFGRAdPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPGWKRRLLRHFGRPRSld 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 192 ELLDKL-LEDNDISSEYKNIITSI------------------INIKGSRSDLETLKQLLEDI---------PESFEALE- 242
Cdd:PRK12295 177 ALLARLaGPRVDPLDEHAGVLAALadeaaaralvedlmsiagISPVGGRSPAEIARRLLEKAalaaaarlpAEALAVLEr 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 243 ------NLDKTLEVLEVF-------------GFDDYV-------VNL-------SIARGLDYYTGIVFEIYVPDLGAEKq 289
Cdd:PRK12295 257 flaisgPPDAALAALRALaadagldldaaldRFEARLaalaargIDLerlrfsaSFGRPLDYYTGFVFEIRAAGNGDPP- 335
|
330 340 350
....*....|....*....|....*....|..
gi 499725512 290 ITGGGTYN--LTALFDSEKVESTGFAFGFDRI 319
Cdd:PRK12295 336 LAGGGRYDglLTRLGAGEPIPAVGFSIWLDRL 367
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
6-318 |
2.99e-19 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 88.87 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 6 PRGTRDFLFEDMEERNYVENTIRNVVENYGFKEIKTPIFEDLELFTTKSGEGIKEEIYHFQDK-GGRDLALRPELTASVS 84
Cdd:PRK12421 10 PDGVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQTFKLIDQlSGRLMGVRADITPQVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 85 RLyNNNLQKSAKPLKMYYFGSCFRyERPQA-GRFREFWQFGIEVIGGVPIYNEAEIIAMANEALTQVGIKNYEINIGHLG 163
Cdd:PRK12421 90 RI-DAHLLNREGVARLCYAGSVLH-TLPQGlFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGVPALHLDLGHVG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 164 IIKGVLNQLNISSQQQTAIIASIDKEDYELLDKLLEDNDISSEYKNIITSIINIKGsrsDLETLKQLLEDIPES----FE 239
Cdd:PRK12421 168 IFRRLAELAGLSPEEEEELFDLLQRKALPELAEVCQNLGVGSDLRRMFYALARLNG---GLEALDRALSVLALQdaaiRQ 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 240 ALENLDKTLEVLEV------FGFDdyVVNLsiaRGLDYYTGIVFEIYVPDLGAEkqITGGGTYNltalfdsekveSTGFA 313
Cdd:PRK12421 245 ALDELKTLAAHLKNrwpelpVSID--LAEL---RGYHYHTGLVFAAYIPGRGQA--LARGGRYD-----------GIGEA 306
|
....*
gi 499725512 314 FGFDR 318
Cdd:PRK12421 307 FGRAR 311
|
|
| 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 ... |
21-129 |
1.10e-17 |
|
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: 81.67 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 21 NYVENTIRNVVENYGFKEIKTPIFEDLELFTtKSG--EGIKEEIYHFQDKG----GRDLALRPELTASVSRLYNNN-LQK 93
Cdd:cd00670 6 RALERFLDDRMAEYGYQEILFPFLAPTVLFF-KGGhlDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFSGEiLSY 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 499725512 94 SAKPLKMYYFGSCFRYERPQA---GRFREFWQFGIEVIG 129
Cdd:cd00670 85 RALPLRLDQIGPCFRHEPSGRrglMRVREFRQVEYVVFG 123
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
20-130 |
8.89e-15 |
|
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: 72.92 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 20 RNYVENTIRNVVENYGFKEIKTPIFEDLELFtTKSGEGIKEEiYHFQDKGGRDLALRPELTASVSRLYNNNLQKSakPLK 99
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLL-EKAGHEPKDL-LPVGAENEEDLYLRPTLEPGLVRLFVSHIRKL--PLR 77
|
90 100 110
....*....|....*....|....*....|...
gi 499725512 100 MYYFGSCFRYERPQAG--RFREFWQFGIEVIGG 130
Cdd:cd00768 78 LAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGE 110
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
336-424 |
1.17e-14 |
|
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: 69.11 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 336 PKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMIGQQEVEDETVTIKDMDSGCQETI 415
Cdd:cd00859 2 VDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETV 81
|
....*....
gi 499725512 416 PQNTVVSEL 424
Cdd:cd00859 82 ALDELVEEL 90
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
23-321 |
9.45e-13 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 68.10 E-value: 9.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 23 VENTIRNVVENYGFKEIKTPIFEDLELFTTKSgegiKEEIYHFQDKGGRDLALRPELTASVSRLYNNNLQKSAKPLKMYY 102
Cdd:PRK12293 25 IENVASEILYENGFEEIVTPFFSYHQHQSIAD----EKELIRFSDEKNHQISLRADSTLDVVRIVTKRLGRSTEHKKWFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 103 FGSCFRYerPQagrfREFWQFGIEVIGGvpiYNEAEIIAMANEALTQVGIKNYeINIGHLGIIKGVLNQLNissqqqtai 182
Cdd:PRK12293 101 IQPVFRY--PS----NEIYQIGAELIGE---EDLSEILNIAAEIFEELELEPI-LQISNIKIPKLVAEILG--------- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 183 iasIDKEDYEL--LDKLLEDNdisseyKNIITSIINIKgsrsDLETLKQLLEDIPESFEalENLDKTLEVLEVFGFDDYV 260
Cdd:PRK12293 162 ---LDIEVFKKgqIEKLLAQN------VPWLNKLVRIK----TLEDLDEVIELVPDEIK--EELEKLKELAESIKYENLV 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499725512 261 VNLSIARGLDYYTGIVFEIYVpdlgAEKQITGGGTYnltalfDSEKVESTGFAFGFDRIME 321
Cdd:PRK12293 227 IAPLYYAKMRYYDDLFFRFFD----GNSTLASGGNY------EIDGISSSGFALYTDNLIE 277
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
337-426 |
1.04e-09 |
|
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: 55.28 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 337 KVLVIPVKK---EFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMIGQQEVEDETVTIKDMDSGCQE 413
Cdd:pfam03129 1 QVVVIPLGEkaeELEEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|...
gi 499725512 414 TIPQNTVVSELLK 426
Cdd:pfam03129 81 TVSLDELVEKLKE 93
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
63-129 |
5.79e-08 |
|
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: 52.41 E-value: 5.79e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499725512 63 YHFQDKGGRDLALRPELTASVSRLYNNNLQKSAK-PLKMYYFGSCFRYERPQA----GRFREFWQFGIEVIG 129
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLRSKDlPLKLAQFGTCFRHEASGDtrglIRVRQFHQDDAHIFH 72
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
20-122 |
3.56e-07 |
|
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: 51.40 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 20 RNYVENTIRNVVENYGFKEIKTPIFEDLELFTTkSG--EGIKEEIYhFQDKGGRDLALRP-------ELTASVSRLYnNN 90
Cdd:cd00771 33 RNELEDFLRELQRKRGYQEVETPIIYNKELWET-SGhwDHYRENMF-PFEEEDEEYGLKPmncpghcLIFKSKPRSY-RD 109
|
90 100 110
....*....|....*....|....*....|....*...
gi 499725512 91 LqksakPLKMYYFGSCFRYErpQAG------RFREFWQ 122
Cdd:cd00771 110 L-----PLRLAEFGTVHRYE--QSGalhgltRVRGFTQ 140
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
338-426 |
5.74e-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: 47.11 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 338 VLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMIGQQEVEDETVTIKDMDSGCQETIPq 417
Cdd:cd00860 4 VVVIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGSMS- 82
|
....*....
gi 499725512 418 ntvVSELLK 426
Cdd:cd00860 83 ---LDEFIE 88
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
26-111 |
3.30e-05 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 46.18 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 26 TIRNVVENY--------GFKEIKTPIFEDLELFTTkSG--EGIKEEIYhFQDKGGRDLALRP-------ELtasvsrlYN 88
Cdd:COG0441 272 IIRRELEDYirekhrkaGYQEVKTPHILDRELWET-SGhwDHYRENMF-PTESDGEEYALKPmncpghiLI-------YK 342
|
90 100
....*....|....*....|....*
gi 499725512 89 NNLqKSAK--PLKMYYFGSCFRYER 111
Cdd:COG0441 343 SGL-RSYRdlPLRLAEFGTVHRYEP 366
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
319-405 |
1.47e-04 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 43.68 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 319 IMEAYHRQNIQVPISSKP-KVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMIGQQEV 397
Cdd:PRK14938 257 LLESIRKQPPTLPDWLNPiQVRILPVKKDFLDFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREV 336
|
....*...
gi 499725512 398 EDETVTIK 405
Cdd:PRK14938 337 KTSTLTVK 344
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
334-426 |
4.81e-03 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 39.37 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 334 SKPKVLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMIGQQEVEDETVTIKDMDSGCQE 413
Cdd:PLN02908 588 SPRQAIVVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHG 667
|
90
....*....|...
gi 499725512 414 TIPQNTVVSELLK 426
Cdd:PLN02908 668 EKKIEELLTEFKE 680
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
338-426 |
5.40e-03 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 39.08 E-value: 5.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 338 VLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLKGKKLKKNLSYANNHNFNKVIMIGQQEVEDETVTIKDMDSGCQETIpq 417
Cdd:PRK03991 502 VRVIPVSERHLDYAEEVADKLEAAGIRVDVDDRDESLGKKIRDAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEM-- 579
|
....*....
gi 499725512 418 ntVVSELLK 426
Cdd:PRK03991 580 --TLEELIE 586
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
338-426 |
9.76e-03 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 38.09 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499725512 338 VLVIPVKKEFKLNAIEVAQQLRAHNIVTDIDLkgkklkknlsyAN--------NHNFNKV---IMIGQQEVEDETVTIKD 406
Cdd:COG0441 542 VVVLPISDKHADYAKEVAKKLRAAGIRVEVDL-----------RNekigykirEAQLQKVpymLVVGDKEVENGTVSVRR 610
|
90 100
....*....|....*....|
gi 499725512 407 MDSGCQETIPQNTVVSELLK 426
Cdd:COG0441 611 RGGGDLGTMSLDEFIARLKE 630
|
|
| |
