|
Name |
Accession |
Description |
Interval |
E-value |
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-410 |
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: 572.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 4 QKPKGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDIVTKEMYDFYDKGDRHITLRPEGT 83
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 84 APVVRSYVENKLFAPevqKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKGVTL 163
Cdd:TIGR00442 81 APVARAVIENKLLLP---KPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 164 HLNSLGNAASRAAYRQALIDYLSPMRETLSKDSQRRLDENPLRVLDSKEKEDKIAVANAPSILDYLDEDSQAHFDAVRSM 243
Cdd:TIGR00442 158 EINSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 244 LEALAIPYVIDTNMVRGLDYYNHTIFEFITEVNQSELTICAGGRYDGLVEYFGGPATPGFGFGLGLERLLLILDKQGVEL 323
Cdd:TIGR00442 238 LDALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 324 PVEEGLDVYIAVLGADANVAALALTQAIRRQGFTVERDYLGRKIKAQFKSADTFKAKVVITLGESEIKAGQAVLKHNQTR 403
Cdd:TIGR00442 318 PPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
gi 757117087 404 QEMTVSF 410
Cdd:TIGR00442 398 EQETVPL 404
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-423 |
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: 545.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 1 MKLQKPKGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDttDIVTKEMYDFYDKGDRHITLRP 80
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 81 EGTAPVVRSYVENKLfapEVQKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKG 160
Cdd:COG0124 80 EGTAPVARAVAEHGN---ELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 161 VTLHLNSLGNAASRAayrQALIDYLS-----PMRETLSKDSQRRLDENPLR-VLDSKEKEDKIAVANAPSILDYLDEDSQ 234
Cdd:COG0124 157 FTLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 235 AHFDAVRSMLEALAIPYVIDTNMVRGLDYYNHTIFEFITEVNQSELTICAGGRYDGLVEYFGGPATPG----------Fg 304
Cdd:COG0124 234 AHFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAvgfaiglerlL- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 305 fglglerllLILDKQGVELPVEEGLDVYIAVLGADANVAALALTQAIRRQGFTVERDYLGRKIKAQFKSADTFKAKVVIT 384
Cdd:COG0124 313 ---------LLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLI 383
|
410 420 430
....*....|....*....|....*....|....*....
gi 757117087 385 LGESEIKAGQAVLKHNQTRQEMTVSFDQIQTDFASIFAE 423
Cdd:COG0124 384 LGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
2-414 |
7.25e-125 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 368.46 E-value: 7.25e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 2 KLQKPKGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDIVTKEMYDFYDKGDRHITLRPE 81
Cdd:CHL00201 3 KIQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLRPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 82 GTAPVVRSYVENKL-FAPEVQKpvkLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKG 160
Cdd:CHL00201 83 GTAGIVRAFIENKMdYHSNLQR---LWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 161 VTLHLNSLGNAASRAAYRQALIDYLSPMRETLSKDSQRRLDENPLRVLDSKEKEDKIAVANAPSILDYLDEDSQAHFDAV 240
Cdd:CHL00201 160 LILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYDV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 241 RSMLEALAIPYVIDTNMVRGLDYYNHTIFEFITEVNQSELTICAGGRYDGLVEYFGGPATPGFGFGLGLERLLLILdKQG 320
Cdd:CHL00201 240 CTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIA-KDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 321 VELPvEEGLDVYIAVLGADANVAALALTQAIRRQGFTVERDYLGRKIKAQFKSADTFKAKVVITLGESEIKAGQAVLKHN 400
Cdd:CHL00201 319 IILP-KQSIDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWL 397
|
410
....*....|....
gi 757117087 401 QTRQEMTVSFDQIQ 414
Cdd:CHL00201 398 DEQVQENAQYSNFK 411
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
17-302 |
7.28e-93 |
|
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: 280.64 E-value: 7.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 17 AAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDttdIVTKEMYDFYDKGDRHITLRPEGTAPVVRSYVENKLF 96
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGD---EVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 97 APevqKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKGVTLHLNSLG------- 169
Cdd:cd00773 79 LP---LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGildgiag 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 170 NAASRAAYRQALIdylspmretlskdsqrrldenplrvldskekedkiavanapsilDYLDEDSQAHFDAVRSMLEAL-- 247
Cdd:cd00773 156 LLEDREEYIERLI--------------------------------------------DKLDKEALAHLEKLLDYLEALgv 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 757117087 248 AIPYVIDTNMVRGLDYYNHTIFEFITEVNQSELTICAGGRYDGLVEYFGGPATPG 302
Cdd:cd00773 192 DIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPA 246
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-303 |
2.98e-37 |
|
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: 137.72 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 8 GTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDivtkEMYDFYDKGDRHITLRPEGTAPVV 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 88 RsYVENKLFAPEVQKpvkLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKGVTLHLNS 167
Cdd:pfam13393 77 R-IDAHRLNRPGPLR---LCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 168 -------LGNAASRAAYRQALIDYLSpmretlSKDS--------QRRLDENPLRVLD-----SKEKEdkiAVANAPSILD 227
Cdd:pfam13393 153 vglvralLEAAGLSEALEEALRAALQ------RKDAaelaelaaEAGLPPALRRALLalpdlYGGPE---VLDEARAALP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 228 YLDE--DSQAHFDAVRSMLEALA--IPYVIDTNMVRGLDYYNHTIFEFITEvnQSELTICAGGRYDGLVEYFGG--PATp 301
Cdd:pfam13393 224 GLPAlqEALDELEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYAP--GVGEPLARGGRYDDLGAAFGRarPAT- 300
|
..
gi 757117087 302 GF 303
Cdd:pfam13393 301 GF 302
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
4-410 |
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: 572.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 4 QKPKGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDIVTKEMYDFYDKGDRHITLRPEGT 83
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 84 APVVRSYVENKLFAPevqKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKGVTL 163
Cdd:TIGR00442 81 APVARAVIENKLLLP---KPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 164 HLNSLGNAASRAAYRQALIDYLSPMRETLSKDSQRRLDENPLRVLDSKEKEDKIAVANAPSILDYLDEDSQAHFDAVRSM 243
Cdd:TIGR00442 158 EINSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKEL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 244 LEALAIPYVIDTNMVRGLDYYNHTIFEFITEVNQSELTICAGGRYDGLVEYFGGPATPGFGFGLGLERLLLILDKQGVEL 323
Cdd:TIGR00442 238 LDALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 324 PVEEGLDVYIAVLGADANVAALALTQAIRRQGFTVERDYLGRKIKAQFKSADTFKAKVVITLGESEIKAGQAVLKHNQTR 403
Cdd:TIGR00442 318 PPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
gi 757117087 404 QEMTVSF 410
Cdd:TIGR00442 398 EQETVPL 404
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-423 |
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: 545.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 1 MKLQKPKGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDttDIVTKEMYDFYDKGDRHITLRP 80
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 81 EGTAPVVRSYVENKLfapEVQKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKG 160
Cdd:COG0124 80 EGTAPVARAVAEHGN---ELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 161 VTLHLNSLGNAASRAayrQALIDYLS-----PMRETLSKDSQRRLDENPLR-VLDSKEKEDKIAVANAPSILDYLDEDSQ 234
Cdd:COG0124 157 FTLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 235 AHFDAVRSMLEALAIPYVIDTNMVRGLDYYNHTIFEFITEVNQSELTICAGGRYDGLVEYFGGPATPG----------Fg 304
Cdd:COG0124 234 AHFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAvgfaiglerlL- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 305 fglglerllLILDKQGVELPVEEGLDVYIAVLGADANVAALALTQAIRRQGFTVERDYLGRKIKAQFKSADTFKAKVVIT 384
Cdd:COG0124 313 ---------LLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLI 383
|
410 420 430
....*....|....*....|....*....|....*....
gi 757117087 385 LGESEIKAGQAVLKHNQTRQEMTVSFDQIQTDFASIFAE 423
Cdd:COG0124 384 LGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
2-414 |
7.25e-125 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 368.46 E-value: 7.25e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 2 KLQKPKGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDIVTKEMYDFYDKGDRHITLRPE 81
Cdd:CHL00201 3 KIQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLRPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 82 GTAPVVRSYVENKL-FAPEVQKpvkLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKG 160
Cdd:CHL00201 83 GTAGIVRAFIENKMdYHSNLQR---LWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 161 VTLHLNSLGNAASRAAYRQALIDYLSPMRETLSKDSQRRLDENPLRVLDSKEKEDKIAVANAPSILDYLDEDSQAHFDAV 240
Cdd:CHL00201 160 LILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYDV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 241 RSMLEALAIPYVIDTNMVRGLDYYNHTIFEFITEVNQSELTICAGGRYDGLVEYFGGPATPGFGFGLGLERLLLILdKQG 320
Cdd:CHL00201 240 CTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIA-KDN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 321 VELPvEEGLDVYIAVLGADANVAALALTQAIRRQGFTVERDYLGRKIKAQFKSADTFKAKVVITLGESEIKAGQAVLKHN 400
Cdd:CHL00201 319 IILP-KQSIDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWL 397
|
410
....*....|....
gi 757117087 401 QTRQEMTVSFDQIQ 414
Cdd:CHL00201 398 DEQVQENAQYSNFK 411
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
17-302 |
7.28e-93 |
|
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: 280.64 E-value: 7.28e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 17 AAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDttdIVTKEMYDFYDKGDRHITLRPEGTAPVVRSYVENKLF 96
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGD---EVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 97 APevqKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKGVTLHLNSLG------- 169
Cdd:cd00773 79 LP---LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGildgiag 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 170 NAASRAAYRQALIdylspmretlskdsqrrldenplrvldskekedkiavanapsilDYLDEDSQAHFDAVRSMLEAL-- 247
Cdd:cd00773 156 LLEDREEYIERLI--------------------------------------------DKLDKEALAHLEKLLDYLEALgv 191
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 757117087 248 AIPYVIDTNMVRGLDYYNHTIFEFITEVNQSELTICAGGRYDGLVEYFGGPATPG 302
Cdd:cd00773 192 DIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPA 246
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
10-303 |
1.56e-47 |
|
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA synthetase, found in Bacillus subtilis, Synechocystis sp., Aquifex aeolicus, and others, are in fact a regulatory subunit of ATP phosphoribosyltransferase, and usually encoded by a gene adjacent to that encoding the catalytic subunit. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273081 [Multi-domain] Cd Length: 313 Bit Score: 165.09 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 10 QDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDivtkEMYDFYDKGDRHITLRPEGTAPVVRS 89
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNE----DLFKLFDQLGRVLGLRPDMTAPIARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 90 YVEnKLfaPEVQKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKGVTLHL---- 165
Cdd:TIGR00443 77 VST-RL--RDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELghvg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 166 -------NSLGNAASRAAYRQALI--DYLSPMRETLSKDSQRRLDENPLRVLD----SKEKEDKI-AVANAPSILDYLDE 231
Cdd:TIGR00443 154 lvralleEAGLPEEAREALREALArkDLVALEELVAELGLSPEVRERLLALPRlrgdGEEVLEEArALAGSETAEAALDE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757117087 232 dsqahFDAVRSMLEALAIP--YVIDTNMVRGLDYYNHTIFE-FITEVNQselTICAGGRYDGLVEYFG--GPATpGF 303
Cdd:TIGR00443 234 -----LEAVLELLEARGVEeyISLDLGLVRGYHYYTGLIFEgYAPGLGA---PLAGGGRYDELLGRFGrpLPAT-GF 301
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
1-365 |
3.60e-47 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 166.19 E-value: 3.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 1 MKLQKPKGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDIvtkEMYDFYDKG-DRHITLR 79
Cdd:PRK12292 1 MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDL---RTFKLVDQLsGRTLGLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 80 PEGTAPVVRSyVENKLfaPEVQKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIK 159
Cdd:PRK12292 78 PDMTAQIARI-AATRL--ANRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 160 GVTLHL-----------NSLGNAASRAAYRQALI--DY--LSPMRETLSKDSQRRLDE-----NPLRVLDskekedkiav 219
Cdd:PRK12292 155 NFTLDLghvglfralleAAGLSEELEEVLRRALAnkDYvaLEELVLDLSEELRDALLAlprlrGGREVLE---------- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 220 aNAPSIldYLDEDSQAHFDAVRSMLEALAIPYV-----IDTNMVRGLDYYNHTIFE-FITEVNQSeltICAGGRYDGLVE 293
Cdd:PRK12292 225 -EARKL--LPSLPIKRALDELEALAEALEKYGYgiplsLDLGLLRHLDYYTGIVFEgYVDGVGNP---IASGGRYDDLLG 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757117087 294 YFGG--PATpGFgfglglerlLLILDK--QGVELPVEEGLDVYIAVLGADANVAALALTQAIRRQGFTVERDYLGR 365
Cdd:PRK12292 299 RFGRarPAT-GF---------SLDLDRllELQLELPVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVLALPGR 364
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
1-413 |
2.15e-43 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 157.20 E-value: 2.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 1 MKLQKPKGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDIVtKEMYDFYDKGDRHITLRP 80
Cdd:PRK12420 2 MEMRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGDEIL-KEIYTLTDQGKRDLALRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 81 EGTAPVVRSYVENklfaPEVQKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKg 160
Cdd:PRK12420 81 DLTIPFAKVVAMN----PNIRLPFKRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 161 VTLHLN----------SLGNAASRAAYRQALIDYLSPM------RETLSKDSQRRLDENPLRVLDSKEKEDKIAVANAPS 224
Cdd:PRK12420 156 VTIQYNnrkllngilqAIGIPTELTSDVILSLDKIEKIgidgvrKDLLERGISEEMADTICNTVLSCLQLSIADFKEAFN 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 225 ilDYLDEDSQAHFDAVRSMLEALAIP--YVIDTNMVRGLDYYNHTIFEFITEVNQSELTICAGGRYDGLVEYFGGP--AT 300
Cdd:PRK12420 236 --NPLVAEGVNELQQLQQYLIALGINenCIFNPFLARGLTMYTGTVYEIFLKDGSITSSIGSGGRYDNIIGAFRGDdmNY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 301 PGFGFGLGLERLLLILDKQGVElpvEEGLDVYIAVLGADAnvAALALTQAIRR-QGFTVERDYLGRKIKAQFKSADTFKA 379
Cdd:PRK12420 314 PTVGISFGLDVIYTALSQKETI---SSTADVFIIPLGTEL--QCLQIAQQLRStTGLKVELELAGRKLKKALNYANKENI 388
|
410 420 430
....*....|....*....|....*....|....
gi 757117087 380 KVVITLGESEIKAGQAVLKHNQTRQEMTVSFDQI 413
Cdd:PRK12420 389 PYVLIIGEEEVSTGTVMLRNMKEGSEVKVPLSSL 422
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
13-303 |
1.33e-41 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 149.17 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 13 LPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDivtKEMYDFYDKGDRHITLRPEGTAPVVRSYVE 92
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVARIAAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 93 NklfAPEVQKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKGVTLHLNSLG--- 169
Cdd:COG3705 78 R---LANRPGPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGlfr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 170 --------NAASRAAYRQAL-------IDYLsPMRETLSKDSQRRLdenpLRVLDSKEKEDKIAVANApsiLDyLDEDSQ 234
Cdd:COG3705 155 allealglSEEQREELRRALarkdaveLEEL-LAELGLSEELAEAL----LALPELYGGEEVLARARA---LL-LDAAIR 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 757117087 235 AHFDAVRSMLEALA-----IPYVIDTNMVRGLDYYNHTIFEFIteVNQSELTICAGGRYDGLVEYFGG--PATpGF 303
Cdd:COG3705 226 AALDELEALAEALAargpdVRLTFDLSELRGYDYYTGIVFEAY--APGVGDPLARGGRYDGLLAAFGRarPAT-GF 298
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
3-414 |
1.07e-40 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 151.05 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 3 LQKPKGTQDILP--VAAAKWQYveDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTtdiVTKEMYDFYDKGDRHITLRP 80
Cdd:PLN02530 70 VNPPKGTRDFPPedMRLRNWLF--DHFREVSRLFGFEEVDAPVLESEELYIRKAGEE---ITDQLYNFEDKGGRRVALRP 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 81 EGTAPVVRSYVENklfAPEVQKPVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGI-- 158
Cdd:PLN02530 145 ELTPSLARLVLQK---GKSLSLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGIts 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 159 ----------KGVTLHLNSLGNAASRAAYRQALIDYLSPM-RETLSKDsqrrLDENPLrvldSKEKEDKIAVANAPSILD 227
Cdd:PLN02530 222 sdvgikvssrKVLQAVLKSYGIPEESFAPVCVIVDKLEKLpREEIEKE----LDTLGV----SEEAIEGILDVLSLKSLD 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 228 YLDEDSQAHFDAVRSM--LEALAIPY------VIDTNMVRGLDYYNHTIFE-FITEvnqSEL-TICAGGRYDGLVEYFGG 297
Cdd:PLN02530 294 DLEALLGADSEAVADLkqLFSLAEAYgyqdwlVFDASVVRGLAYYTGIVFEgFDRA---GKLrAICGGGRYDRLLSTFGG 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 298 PATP----GFgfglglerllliLDKQGVELPVEEGL--------DVYIAVLGADANVAALALTQAIRRQGFTVERDYLGR 365
Cdd:PLN02530 371 EDTPacgfGF------------GDAVIVELLKEKGLlpelphqvDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLEPK 438
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 757117087 366 KIKAQFKSADTFKAKVVITLGESEIKAGQAVLKHNQTRQEMTVSFDQIQ 414
Cdd:PLN02530 439 KLKWVFKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDELE 487
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-303 |
2.98e-37 |
|
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: 137.72 E-value: 2.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 8 GTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDivtkEMYDFYDKGDRHITLRPEGTAPVV 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 88 RsYVENKLFAPEVQKpvkLYYIGSMFRYERPQVGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGIKGVTLHLNS 167
Cdd:pfam13393 77 R-IDAHRLNRPGPLR---LCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGH 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 168 -------LGNAASRAAYRQALIDYLSpmretlSKDS--------QRRLDENPLRVLD-----SKEKEdkiAVANAPSILD 227
Cdd:pfam13393 153 vglvralLEAAGLSEALEEALRAALQ------RKDAaelaelaaEAGLPPALRRALLalpdlYGGPE---VLDEARAALP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 228 YLDE--DSQAHFDAVRSMLEALA--IPYVIDTNMVRGLDYYNHTIFEFITEvnQSELTICAGGRYDGLVEYFGG--PATp 301
Cdd:pfam13393 224 GLPAlqEALDELEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYAP--GVGEPLARGGRYDDLGAAFGRarPAT- 300
|
..
gi 757117087 302 GF 303
Cdd:pfam13393 301 GF 302
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
328-413 |
1.40e-27 |
|
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: 104.93 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 328 GLDVYIAVLGADANVAALALTQAIRRQGFTVERDYLGRKIKAQFKSADTFKAKVVITLGESEIKAGQAVLKHNQTRQEMT 407
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQET 80
|
....*.
gi 757117087 408 VSFDQI 413
Cdd:cd00859 81 VALDEL 86
|
|
| 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 ... |
16-216 |
2.19e-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: 2.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 16 AAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRsvGDTTDIVTKEMYDFYDKG----DRHITLRPEGTAPVVRSYV 91
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFK--GGHLDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 92 ENKLFAPevQKPVKLYYIGSMFRYERPQV---GRSREFHQIGVECFG--SANPATDVETIAMAYHLFERLGIKgVTLHLN 166
Cdd:cd00670 79 GEILSYR--ALPLRLDQIGPCFRHEPSGRrglMRVREFRQVEYVVFGepEEAEEERREWLELAEEIARELGLP-VRVVVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 757117087 167 SLGNAASRA-----AYRQALIDYlspmrETLSKDSQR--------RLDENPLRVLDSKEKEDK 216
Cdd:cd00670 156 DDPFFGRGGkrgldAGRETVVEF-----ELLLPLPGRaketavgsANVHLDHFGASFKIDEDG 213
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
6-423 |
6.48e-22 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 98.42 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 6 PKGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSVGDTTDIVtkemYDFYDKGDRHITLRPEGTAP 85
Cdd:PLN02972 330 PKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLI----YDLADQGGELCSLRYDLTVP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 86 VVRSYVENKLFApevqkpVKLYYIGSMFRYERPQVGRSREFHQIGVECFGSANP-ATDVETIAMAYHLFERLGIKGVTLH 164
Cdd:PLN02972 406 FARYVAMNGITS------FKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPmGPDFEIIKVLTELLDELDIGTYEVK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 165 LNSLG--------NAASRAAYRQ--ALIDYLSpmRETLSKDSQRRLDEN-------------------PLRVLDSKEKED 215
Cdd:PLN02972 480 LNHRKlldgmleiCGVPPEKFRTicSSIDKLD--KQSFEQVKKEMVEEKglsnetadkignfvkergpPLELLSKLRQEG 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 216 KIAVANAPSIlDYLDEDSqAHFDAVRSMLEALAIpyVIDTNMVRGLDYYNHTIFEFI---TEVNqselTICAGGRYDGLV 292
Cdd:PLN02972 558 SEFLGNASSR-AALDELE-IMFKALEKSKAIGKI--VFDLSLARGLDYYTGVIYEAVfkgAQVG----SIAAGGRYDNLV 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 293 EYFGGPATPGFGFGLGLERLLLILDKQ-----GVELPVEEglDVYIAVLGADANVAALALTQAIRRQGFTVERDyLGRKI 367
Cdd:PLN02972 630 GMFSGKQVPAVGVSLGIERVFAIMEQQeeeksQVIRPTET--EVLVSIIGDDKLALAAELVSELWNAGIKAEYK-VSTRK 706
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 757117087 368 KAQFKSADTFKAKVVITLGESEIKAGQAVLKHNQTRQEMTVSfdqiQTDFASIFAE 423
Cdd:PLN02972 707 AKHLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVD----RTCFVQELKA 758
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
20-187 |
7.67e-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: 70.22 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 20 WQYVEDVARETFKQYHYGEIRTPMFEHyevisRSVGDTTDIVTKEMYDFYDKGDRHITLRPEGTAPVVRSYVENKLFAPE 99
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVER-----EPLLEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRKLPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 100 vqkpvKLYYIGSMFRYERPQVG--RSREFHQIGVECFGS--ANPATDVETIAMAYHLFERLGIK-GVTLHLNSLGNAASR 174
Cdd:cd00768 77 -----RLAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGEdgEEASEFEELIELTEELLRALGIKlDIVFVEKTPGEFSPG 151
|
170
....*....|...
gi 757117087 175 AAYRQALIDYLSP 187
Cdd:cd00768 152 GAGPGFEIEVDHP 164
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
78-299 |
1.78e-13 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 71.50 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 78 LRPEGTAPVVRSYVENKLFAPEvqkpvKLYYIGSMFRYerpQVGRSREFHQIGVECFGSANP-ATDVETIAMAYHLFERL 156
Cdd:PRK12295 62 LRPDFTIPVCRRHIATAGGEPA-----RYAYLGEVFRQ---RRDRASEFLQAGIESFGRADPaAADAEVLALALEALAAL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 157 GIKGVTLhlnSLGNAASRAAYRQALiDYLSPMRETLSKD--SQRRLDE-------NPLRVLDSKEK-------------- 213
Cdd:PRK12295 134 GPGDLEV---RLGDVGLFAALVDAL-GLPPGWKRRLLRHfgRPRSLDAllarlagPRVDPLDEHAGvlaaladeaaaral 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 214 -EDKIAVANAPS--------ILDYLDEDSQAH---------------FDAVR-------SMLEALAIPYVIDTNMV---- 258
Cdd:PRK12295 210 vEDLMSIAGISPvggrspaeIARRLLEKAALAaaarlpaealavlerFLAISgppdaalAALRALAADAGLDLDAAldrf 289
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757117087 259 ------------------------RGLDYYNHTIFEFITEVNqSELTICAGGRYDGLVEYFGGPA 299
Cdd:PRK12295 290 earlaalaargidlerlrfsasfgRPLDYYTGFVFEIRAAGN-GDPPLAGGGRYDGLLTRLGAGE 353
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
66-171 |
5.70e-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: 63.97 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 66 YDFYDKGDRHITLRPEGTAPVVRSYVENKLfaPEVQKPVKLYYIGSMFRYERPQ----VGRSREFHQIGVECFGSANPAT 141
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGL--RSKDLPLKLAQFGTCFRHEASGdtrgLIRVRQFHQDDAHIFHAPGQSP 78
|
90 100 110
....*....|....*....|....*....|...
gi 757117087 142 DV--ETIAMAYHLFERLGIKG-VTLHLNSLGNA 171
Cdd:pfam00587 79 DEleDYIKLIDRVYSRLGLEVrVVRLSNSDGSA 111
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
6-358 |
1.10e-11 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 66.15 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 6 PKGTQDILPVAAAKwqyVEDVARETFKQYH---YGEIRTPMFEHYEVISRSVGDTTDIVTkemYDFYDK-GDRHITLRPE 81
Cdd:PRK12421 10 PDGVADVLPEEAQK---IERLRRRLLDLFAsrgYQLVMPPLIEYLESLLTGAGQDLKLQT---FKLIDQlSGRLMGVRAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 82 GTAPVVR--SYVENklfapeVQKPVKLYYIGSMFRyERPQ-VGRSREFHQIGVECFGSANPATDVETIAMAYHLFERLGI 158
Cdd:PRK12421 84 ITPQVARidAHLLN------REGVARLCYAGSVLH-TLPQgLFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 159 KGvtLHLNsLGNAA-SRAAYRQAlidYLSPMRE-TLSKDSQRR--------LDENPlrvLDSKEKEDKIAVANAPSILDY 228
Cdd:PRK12421 157 PA--LHLD-LGHVGiFRRLAELA---GLSPEEEeELFDLLQRKalpelaevCQNLG---VGSDLRRMFYALARLNGGLEA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 229 LDE--------DSQAH--FDAVRSMLEAL-----AIPYVIDTNMVRGldYYNHTIFEFITEVNQSELTICAGGRYDGLVE 293
Cdd:PRK12421 228 LDRalsvlalqDAAIRqaLDELKTLAAHLknrwpELPVSIDLAELRG--YHYHTGLVFAAYIPGRGQALARGGRYDGIGE 305
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 757117087 294 YFGG--PATpGFGFGLGLErlllildkqGVELPVEEGLDVYIAVLGADANVAalALTQAIRRQGFTV 358
Cdd:PRK12421 306 AFGRarPAT-GFSMDLKEL---------LALQFLEEEAGAILAPWGDDPDLL--AAIAELRQQGERV 360
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
23-159 |
1.83e-10 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 61.16 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 23 VEDVARETFKQYHYGEIRTPMFEHYEviSRSVGDTtdivtKEMYDFYDKGDRHITLRPEGTAPVVRsYVENKLfaPEVQK 102
Cdd:PRK12293 25 IENVASEILYENGFEEIVTPFFSYHQ--HQSIADE-----KELIRFSDEKNHQISLRADSTLDVVR-IVTKRL--GRSTE 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 757117087 103 PVKLYYIGSMFRYerPqvgrSREFHQIGVECFGSANPAtdvETIAMAYHLFERLGIK 159
Cdd:PRK12293 95 HKKWFYIQPVFRY--P----SNEIYQIGAELIGEEDLS---EILNIAAEIFEELELE 142
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
328-413 |
6.36e-09 |
|
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: 52.79 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 328 GLDVYIAVLGAD---ANVAALALTQAIRRQGFTVERDYLGRKIKAQFKSADTFKAKVVITLGESEIKAGQAVLKHNQTRQ 404
Cdd:cd00738 1 PIDVAIVPLTDPrveAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGE 80
|
....*....
gi 757117087 405 EMTVSFDQI 413
Cdd:cd00738 81 SETLHVDEL 89
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
330-413 |
9.87e-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: 52.20 E-value: 9.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 330 DVYIAVLGADANVA---ALALTQAIRRQGFTVERDYLGRKIKAQFKSADTFKAKVVITLGESEIKAGQAVLKHNQTRQEM 406
Cdd:pfam03129 1 QVVVIPLGEKAEELeeyAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
....*..
gi 757117087 407 TVSFDQI 413
Cdd:pfam03129 81 TVSLDEL 87
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
7-126 |
1.75e-05 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 46.21 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757117087 7 KGTQDILPVAAAKWQYVEDVARETFKQYHYGEIRTPMFEHYEVISRSvGDTTDIVTKEMYDFYDKGDRHI----TLRPeg 82
Cdd:cd00772 22 RGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFLEKE-AEHDEGFSKELAVFKDAGDEELeedfALRP-- 98
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 757117087 83 TAPVVRSYVENKLFAPEVQKPVKLYYIGSMFRYE-RPQVG--RSREF 126
Cdd:cd00772 99 TLEENIGEIAAKFIKSWKDLPQHLNQIGNKFRDEiRPRFGflRAREF 145
|
|
| |
