|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
13-427 |
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: 535.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 13 FSAPKGVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGEstDVVTKEMYTFADRGDRSVTLRPEG 92
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLRPEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 93 TAGVMRAVIEHNLDRgQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLE 172
Cdd:COG0124 82 TAPVARAVAEHGNEL-PFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 173 LTSLGDNTCRPEyraKLQEFLFELP-------LDEETRHRANINPLR-VLDDKRPEMQEMLADAPLMLDHLSDSARSHFE 244
Cdd:COG0124 161 INSRGLPEERAE---ALLRYLDKLDkighedvLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLAHFE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 245 AVTGLLDDMKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAQSGIGGGGRYDGLMAQLGGQELSGIGFGLGVDRALLALEA 324
Cdd:COG0124 238 EVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLLLEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 325 EGKQASDGRRVDVYGVALGEEAAHTMAVQINKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLK 404
Cdd:COG0124 318 LGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANGTVTLK 397
|
410 420
....*....|....*....|...
gi 740843628 405 DLESHEQHAVALDALVQELQSRI 427
Cdd:COG0124 398 DLATGEQETVPLDELVEYLKELL 420
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
14-416 |
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: 523.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 14 SAPKGVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGESTDVVTKEMYTFADRGDRSVTLRPEGT 93
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 94 AGVMRAVIEHNLDRgQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLEL 173
Cdd:TIGR00442 81 APVARAVIENKLLL-PKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 174 TSLGDNTCRPEYRAKLQEFL--FELPLDEETRHRANINPLRVLDDKRPEMQEMLADAPLMLDHLSDSARSHFEAVTGLLD 251
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLdkHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 252 DMKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAQSGIGGGGRYDGLMAQLGGQELSGIGFGLGVDRALLALEAEGKQASD 331
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 332 GRRVDVYGVALGEEAAHTMAVQINKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQ 411
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQ 399
|
....*
gi 740843628 412 HAVAL 416
Cdd:TIGR00442 400 ETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
15-427 |
6.96e-103 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 312.22 E-value: 6.96e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 15 APKGVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGESTDVVTKEMYTFADRGDRSVTLRPEGTA 94
Cdd:CHL00201 6 AIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLRPEGTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 95 GVMRAVIEHNLDRGQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLELT 174
Cdd:CHL00201 86 GIVRAFIENKMDYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKNLILDIN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 175 SLGDNTCRPEYRAKLQEFL--FELPLDEETRHRANINPLRVLDDKRPEMQEMLADAPLMLDHLSDSARSHFEAVTGLLDD 252
Cdd:CHL00201 166 SIGKLEDRQSYQLKLVEYLsqYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYDVCTYLNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 253 MKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAQSGIGGGGRYDGLMAQLGGQELSGIGFGLGVDRALLAleAEGKQASDG 332
Cdd:CHL00201 246 LNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLI--AKDNIILPK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 333 RRVDVYGVALGEEAAHTMAVQINKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQH 412
Cdd:CHL00201 324 QSIDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQE 403
|
410
....*....|....*...
gi 740843628 413 AVALDALVQE---LQSRI 427
Cdd:CHL00201 404 NAQYSNFKQEisyLKKKI 421
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
27-323 |
1.41e-86 |
|
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: 264.46 E-value: 1.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 27 SREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGestDVVTKEMYTFADRGDRSVTLRPEGTAGVMRAVIEHNLD 106
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSG---DEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 107 RgQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLELTSLGdntcrpeyr 186
Cdd:cd00773 79 L-PLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRG--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 187 aKLQEFLFELPLDEETRHRAninplrvlddkrpemqemladaplmLDHLSDSARSHFEAVTGLLDDMKV--PYVINPRMV 264
Cdd:cd00773 149 -ILDGIAGLLEDREEYIERL-------------------------IDKLDKEALAHLEKLLDYLEALGVdiKYSIDLSLV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 740843628 265 RGLDYYTKTCFEFVHDGLGAQSGIGGGGRYDGLMAQLGGQELSGIGFGLGVDRALLALE 323
Cdd:cd00773 203 RGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
18-317 |
1.78e-32 |
|
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: 124.62 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 18 GVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGESTDvvtkEMYTFADRGDRSVTLRPEGTAGVM 97
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 98 RAViEHNLDRgQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLELTS-- 175
Cdd:pfam13393 77 RID-AHRLNR-PGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHvg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 176 -----LGDNTCRPEYRAKLQEFLF------------ELPLDEETRHRANINP-----LRVLDDKRPEmqemLADAPLMLD 233
Cdd:pfam13393 155 lvralLEAAGLSEALEEALRAALQrkdaaelaelaaEAGLPPALRRALLALPdlyggPEVLDEARAA----LPGLPALQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 234 hlsdsARSHFEAVTGLLDD--MKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAQsgIGGGGRYDGLMAQLGGQElSGIGF 311
Cdd:pfam13393 231 -----ALDELEALAALLEAlgDGVRLTFDLAELRGYEYYTGIVFAAYAPGVGEP--LARGGRYDDLGAAFGRAR-PATGF 302
|
....*.
gi 740843628 312 GLGVDR 317
Cdd:pfam13393 303 SLDLEA 308
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
13-427 |
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: 535.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 13 FSAPKGVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGEstDVVTKEMYTFADRGDRSVTLRPEG 92
Cdd:COG0124 4 IQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLRPEG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 93 TAGVMRAVIEHNLDRgQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLE 172
Cdd:COG0124 82 TAPVARAVAEHGNEL-PFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDFTLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 173 LTSLGDNTCRPEyraKLQEFLFELP-------LDEETRHRANINPLR-VLDDKRPEMQEMLADAPLMLDHLSDSARSHFE 244
Cdd:COG0124 161 INSRGLPEERAE---ALLRYLDKLDkighedvLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLAHFE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 245 AVTGLLDDMKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAQSGIGGGGRYDGLMAQLGGQELSGIGFGLGVDRALLALEA 324
Cdd:COG0124 238 EVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLLLEE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 325 EGKQASDGRRVDVYGVALGEEAAHTMAVQINKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLK 404
Cdd:COG0124 318 LGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANGTVTLK 397
|
410 420
....*....|....*....|...
gi 740843628 405 DLESHEQHAVALDALVQELQSRI 427
Cdd:COG0124 398 DLATGEQETVPLDELVEYLKELL 420
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
14-416 |
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: 523.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 14 SAPKGVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGESTDVVTKEMYTFADRGDRSVTLRPEGT 93
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 94 AGVMRAVIEHNLDRgQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLEL 173
Cdd:TIGR00442 81 APVARAVIENKLLL-PKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 174 TSLGDNTCRPEYRAKLQEFL--FELPLDEETRHRANINPLRVLDDKRPEMQEMLADAPLMLDHLSDSARSHFEAVTGLLD 251
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLdkHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 252 DMKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAQSGIGGGGRYDGLMAQLGGQELSGIGFGLGVDRALLALEAEGKQASD 331
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 332 GRRVDVYGVALGEEAAHTMAVQINKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQ 411
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQ 399
|
....*
gi 740843628 412 HAVAL 416
Cdd:TIGR00442 400 ETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
15-427 |
6.96e-103 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 312.22 E-value: 6.96e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 15 APKGVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGESTDVVTKEMYTFADRGDRSVTLRPEGTA 94
Cdd:CHL00201 6 AIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLRPEGTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 95 GVMRAVIEHNLDRGQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLELT 174
Cdd:CHL00201 86 GIVRAFIENKMDYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKNLILDIN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 175 SLGDNTCRPEYRAKLQEFL--FELPLDEETRHRANINPLRVLDDKRPEMQEMLADAPLMLDHLSDSARSHFEAVTGLLDD 252
Cdd:CHL00201 166 SIGKLEDRQSYQLKLVEYLsqYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYDVCTYLNL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 253 MKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAQSGIGGGGRYDGLMAQLGGQELSGIGFGLGVDRALLAleAEGKQASDG 332
Cdd:CHL00201 246 LNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLI--AKDNIILPK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 333 RRVDVYGVALGEEAAHTMAVQINKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQH 412
Cdd:CHL00201 324 QSIDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQVQE 403
|
410
....*....|....*...
gi 740843628 413 AVALDALVQE---LQSRI 427
Cdd:CHL00201 404 NAQYSNFKQEisyLKKKI 421
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
27-323 |
1.41e-86 |
|
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: 264.46 E-value: 1.41e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 27 SREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGestDVVTKEMYTFADRGDRSVTLRPEGTAGVMRAVIEHNLD 106
Cdd:cd00773 2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSG---DEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 107 RgQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLELTSLGdntcrpeyr 186
Cdd:cd00773 79 L-PLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRG--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 187 aKLQEFLFELPLDEETRHRAninplrvlddkrpemqemladaplmLDHLSDSARSHFEAVTGLLDDMKV--PYVINPRMV 264
Cdd:cd00773 149 -ILDGIAGLLEDREEYIERL-------------------------IDKLDKEALAHLEKLLDYLEALGVdiKYSIDLSLV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 740843628 265 RGLDYYTKTCFEFVHDGLGAQSGIGGGGRYDGLMAQLGGQELSGIGFGLGVDRALLALE 323
Cdd:cd00773 203 RGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
21-323 |
4.59e-46 |
|
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: 161.24 E-value: 4.59e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 21 DYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGESTDvvtkEMYTFADRGDRSVTLRPEGTAGVMRAV 100
Cdd:TIGR00443 2 DLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNE----DLFKLFDQLGRVLGLRPDMTAPIARLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 101 IEHnLDRGQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLELTS----- 175
Cdd:TIGR00443 78 STR-LRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELGHvglvr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 176 --LGDNTCRPEYRAKLQEFLFELPLDEETRHRANINPLRVLDDKRPEMQEMLADAPLMLDHLSDSARS--------HFEA 245
Cdd:TIGR00443 157 alLEEAGLPEEAREALREALARKDLVALEELVAELGLSPEVRERLLALPRLRGDGEEVLEEARALAGSetaeaaldELEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 246 VTGLLDD--MKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAQsgIGGGGRYDGLMAQLgGQELSGIGFGLGVDRALLALE 323
Cdd:TIGR00443 237 VLELLEArgVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAP--LAGGGRYDELLGRF-GRPLPATGFALNLERLLEALT 313
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
3-419 |
7.13e-46 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 165.30 E-value: 7.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 3 SSQKPKKLKPFSAPKGVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGEStdvVTKEMYTFADRG 82
Cdd:PLN02530 60 VQEDGKPKIDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEE---ITDQLYNFEDKG 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 83 DRSVTLRPEGTAGVMRAVIEhnldRGQ---LPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADA 159
Cdd:PLN02530 137 GRRVALRPELTPSLARLVLQ----KGKslsLPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVT 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 160 CFRGIGLegfrlelTSlGDNTCRPEYRAKLQEFLFELPLDEETrhranINPLRVLDDK-----RPEMQEMLADAPL---- 230
Cdd:PLN02530 213 FFKRVGI-------TS-SDVGIKVSSRKVLQAVLKSYGIPEES-----FAPVCVIVDKleklpREEIEKELDTLGVseea 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 231 ---MLDHLSDSARSHFEAVTG----LLDDMKVPY------------VINPRMVRGLDYYTKTCFE-FvhDGLGAQSGIGG 290
Cdd:PLN02530 280 iegILDVLSLKSLDDLEALLGadseAVADLKQLFslaeaygyqdwlVFDASVVRGLAYYTGIVFEgF--DRAGKLRAICG 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 291 GGRYDGLMAQLGGQELSGIGFGLGvDRALLALEAE-GKQASDGRRVDVYGVALGEE---AAHTMAVQinkLRQAGIRADM 366
Cdd:PLN02530 358 GGRYDRLLSTFGGEDTPACGFGFG-DAVIVELLKEkGLLPELPHQVDDVVFALDEDlqgAAAGVASR---LREKGRSVDL 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 740843628 367 SYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQHAVALDAL 419
Cdd:PLN02530 434 VLEPKKLKWVFKHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDEL 486
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
24-325 |
5.77e-41 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 147.63 E-value: 5.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 24 PPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGESTDvvtKEMYTFADRGDRSVTLRPEGTAGVMRAVIeH 103
Cdd:COG3705 2 PEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVARIAA-T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 104 NLDRGQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLELTSLGdntcrp 183
Cdd:COG3705 78 RLANRPGPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVG------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 184 eyraKLQEFLFELPLDEETRHRAninpLRVLDDK-RPEMQEMLADAP---------------------------LMLDHL 235
Cdd:COG3705 152 ----LFRALLEALGLSEEQREEL----RRALARKdAVELEELLAELGlseelaeallalpelyggeevlararaLLLDAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 236 SDSARSHFEAVTGLLDDM--KVPYVINPRMVRGLDYYTKTCFEFVHDGLG---AQSgigggGRYDGLMAQLgGQELSGIG 310
Cdd:COG3705 224 IRAALDELEALAEALAARgpDVRLTFDLSELRGYDYYTGIVFEAYAPGVGdplARG-----GRYDGLLAAF-GRARPATG 297
|
330
....*....|....*
gi 740843628 311 FGLGVDRALLALEAE 325
Cdd:COG3705 298 FSLDLDRLLRALPAA 312
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
16-384 |
5.67e-37 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 138.85 E-value: 5.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 16 PKGVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFE--ETglfaRGVGESTDVVTKeMYTFADRG-DRSVTLRPEG 92
Cdd:PRK12292 6 PEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEylDT----LLAGGGAILDLR-TFKLVDQLsGRTLGLRPDM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 93 TAGVMRAViEHNLDRGQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLE 172
Cdd:PRK12292 81 TAQIARIA-ATRLANRPGPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 173 L-------TSLGDNTCRPEYRAKLQEFLFEL----------PLDEETRHRANI-----NPLRVLDDKRpemqEMLADAPL 230
Cdd:PRK12292 160 LghvglfrALLEAAGLSEELEEVLRRALANKdyvaleelvlDLSEELRDALLAlprlrGGREVLEEAR----KLLPSLPI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 231 M--LDHLsdsarshfEAVTGLLDD--MKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAqsGIGGGGRYDGLMAQLGGQeL 306
Cdd:PRK12292 236 KraLDEL--------EALAEALEKygYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGN--PIASGGRYDDLLGRFGRA-R 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740843628 307 SGIGFGLGVDRaLLALEAEGKQASDGRRVDVYGVALGEEAAHtmavQINKLRQAGIRADMSYGGRGLKGAMKGADRAG 384
Cdd:PRK12292 305 PATGFSLDLDR-LLELQLELPVEARKDLVIAPDSEALAAALA----AAQELRKKGEIVVLALPGRNFEDAREYARDRQ 377
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
17-419 |
3.19e-36 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 137.55 E-value: 3.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 17 KGVPDYVPpvsrEFEAVRN----SFQHRARLAGYEHIELPIFEETGLFARGVGESTDVVtKEMYTFADRGDRSVTLRPEG 92
Cdd:PRK12420 8 KGTKDYLP----EEQVLRNkikrALEDVFERYGCKPLETPTLNMYELMSSKYGGGDEIL-KEIYTLTDQGKRDLALRYDL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 93 T---AGVMraVIEHNLdrgQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLE-- 167
Cdd:PRK12420 83 TipfAKVV--AMNPNI---RLPFKRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLEvt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 168 ----------------GFRLELTS-----------LGDNTCRPEYRAK-----LQEFLFELPLDEEtrhRANINPLRVLD 215
Cdd:PRK12420 158 iqynnrkllngilqaiGIPTELTSdvilsldkiekIGIDGVRKDLLERgiseeMADTICNTVLSCL---QLSIADFKEAF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 216 DKrPEMQEMLADAPLMLDHLSdsarshfeaVTGLLDDMkvpyVINPRMVRGLDYYTKTCFE-FVHDGLgAQSGIGGGGRY 294
Cdd:PRK12420 235 NN-PLVAEGVNELQQLQQYLI---------ALGINENC----IFNPFLARGLTMYTGTVYEiFLKDGS-ITSSIGSGGRY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 295 DGLMAQLGGQELS----GIGFGLgvDRALLALEAEGKQASdgrRVDVYGVALGEEA-AHTMAVQInkLRQAGIRADMSYG 369
Cdd:PRK12420 300 DNIIGAFRGDDMNyptvGISFGL--DVIYTALSQKETISS---TADVFIIPLGTELqCLQIAQQL--RSTTGLKVELELA 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 740843628 370 GRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQHAVALDAL 419
Cdd:PRK12420 373 GRKLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVPLSSL 422
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
18-317 |
1.78e-32 |
|
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: 124.62 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 18 GVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGESTDvvtkEMYTFADRGDRSVTLRPEGTAGVM 97
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 98 RAViEHNLDRgQLPVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRLELTS-- 175
Cdd:pfam13393 77 RID-AHRLNR-PGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHvg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 176 -----LGDNTCRPEYRAKLQEFLF------------ELPLDEETRHRANINP-----LRVLDDKRPEmqemLADAPLMLD 233
Cdd:pfam13393 155 lvralLEAAGLSEALEEALRAALQrkdaaelaelaaEAGLPPALRRALLALPdlyggPEVLDEARAA----LPGLPALQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 234 hlsdsARSHFEAVTGLLDD--MKVPYVINPRMVRGLDYYTKTCFEFVHDGLGAQsgIGGGGRYDGLMAQLGGQElSGIGF 311
Cdd:pfam13393 231 -----ALDELEALAALLEAlgDGVRLTFDLAELRGYEYYTGIVFAAYAPGVGEP--LARGGRYDDLGAAFGRAR-PATGF 302
|
....*.
gi 740843628 312 GLGVDR 317
Cdd:pfam13393 303 SLDLEA 308
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
334-424 |
2.47e-31 |
|
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: 114.94 E-value: 2.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 334 RVDVYGVALGEEAAHTMAVQINKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQHA 413
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQET 80
|
90
....*....|.
gi 740843628 414 VALDALVQELQ 424
Cdd:cd00859 81 VALDELVEELK 91
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
16-427 |
2.27e-19 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 90.72 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 16 PKGVPDYVPPV----SREFEAVRNSFQHRARLAgyehIELPIFEETGLFARGVGESTdvvtKEMYTFADRGDRSVTLRPE 91
Cdd:PLN02972 330 PKGTRDFAKEQmairEKAFSIITSVFKRHGATA----LDTPVFELRETLMGKYGEDS----KLIYDLADQGGELCSLRYD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 92 GTAGVMRAVIEHNLDRgqlpVKLSYAGPFFRYERPQAGRYRQLQQVGVEAIGVDDPAL-DAEVI---------------- 154
Cdd:PLN02972 402 LTVPFARYVAMNGITS----FKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPMGpDFEIIkvltelldeldigtye 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 155 ------ALADACFR--GIGLEGFRLELTSLgDNTCRPEYRAKLQEFLFELPLDEETRHRANI------NPLRVLDDKRPE 220
Cdd:PLN02972 478 vklnhrKLLDGMLEicGVPPEKFRTICSSI-DKLDKQSFEQVKKEMVEEKGLSNETADKIGNfvkergPPLELLSKLRQE 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 221 mqemlaDAPLMLDHLSDSARSHFEAVTGLLDDMKV--PYVINPRMVRGLDYYTKTCFEFVHDGLGAQSGIGGGgRYDGLM 298
Cdd:PLN02972 557 ------GSEFLGNASSRAALDELEIMFKALEKSKAigKIVFDLSLARGLDYYTGVIYEAVFKGAQVGSIAAGG-RYDNLV 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 299 AQLGGQELSGIGFGLGVDRALLALEAEGKQASDGRR---VDVYGVALGEEAAHTMAVQINKLRQAGIRADMSYGGRgLKG 375
Cdd:PLN02972 630 GMFSGKQVPAVGVSLGIERVFAIMEQQEEEKSQVIRpteTEVLVSIIGDDKLALAAELVSELWNAGIKAEYKVSTR-KAK 708
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 740843628 376 AMKGADRAGARFALVLGESELAAGEVQLKDLESHEQHAVALDALVQELQSRI 427
Cdd:PLN02972 709 HLKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAEL 760
|
|
| 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 ... |
45-178 |
1.45e-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: 81.28 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 45 GYEHIELPIFEETGLFARGVgeSTDVVTKEMYTFADRG----DRSVTLRPEGTAGVMRAVIEHNLDRGQLPVKLSYAGPF 120
Cdd:cd00670 20 GYQEILFPFLAPTVLFFKGG--HLDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFSGEILSYRALPLRLDQIGPC 97
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740843628 121 FRYERPQA---GRYRQLQQVGVEAIGVD--DPALDAEVIALADACFRGIGLEgFRLELTSLGD 178
Cdd:cd00670 98 FRHEPSGRrglMRVREFRQVEYVVFGEPeeAEEERREWLELAEEIARELGLP-VRVVVADDPF 159
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
29-325 |
1.22e-13 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 71.89 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 29 EFEAVRNSFQHrarlAGYEHIELPIFEETGLFARGVGEStdvVTKEMYTFADRGDRSVTLRPEGTAGVMRAVIEHNldrG 108
Cdd:PRK12295 10 AAEALLASFEA----AGAVRVDPPILQPAEPFLDLSGED---IRRRIFVTSDENGEELCLRPDFTIPVCRRHIATA---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 109 QLPVKLSYAGPFFRYERPQAGRYRQlqqVGVEAIG-VDDPALDAEVIALADACFRGIGLEgfRLELTsLGD--------- 178
Cdd:PRK12295 80 GEPARYAYLGEVFRQRRDRASEFLQ---AGIESFGrADPAAADAEVLALALEALAALGPG--DLEVR-LGDvglfaalvd 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 179 --------------NTCRPEYRAKLQEFLFELPLDEETRHRANINPLRVLDDKRPEMQEMLADA---------------- 228
Cdd:PRK12295 154 alglppgwkrrllrHFGRPRSLDALLARLAGPRVDPLDEHAGVLAALADEAAARALVEDLMSIAgispvggrspaeiarr 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 229 -------------------------------PLMLDHLSDSARSH----------FEAVTGLLDDMKVP---YVINPRMV 264
Cdd:PRK12295 234 llekaalaaaarlpaealavlerflaisgppDAALAALRALAADAgldldaaldrFEARLAALAARGIDlerLRFSASFG 313
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 740843628 265 RGLDYYTKTCFEFVHDGLGAQsGIGGGGRYDGLMAQLG-GQELSGIGFGLGVDRaLLALEAE 325
Cdd:PRK12295 314 RPLDYYTGFVFEIRAAGNGDP-PLAGGGRYDGLLTRLGaGEPIPAVGFSIWLDR-LAALGGA 373
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
336-426 |
4.23e-13 |
|
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: 64.91 E-value: 4.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 336 DVYGVALGE--EAAHTMAVQI-NKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQH 412
Cdd:pfam03129 1 QVVVIPLGEkaEELEEYAQKLaEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|....
gi 740843628 413 AVALDALVQELQSR 426
Cdd:pfam03129 81 TVSLDELVEKLKEL 94
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
76-173 |
3.01e-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: 64.74 E-value: 3.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 76 YTFADRGDRSVTLRPEGTAGVMRAVIEHNLDRGQLPVKLSYAGPFFRYERPQA----GRYRQLQQVGVEAIGVDDPALD- 150
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLRSKDLPLKLAQFGTCFRHEASGDtrglIRVRQFHQDDAHIFHAPGQSPDe 80
|
90 100
....*....|....*....|....
gi 740843628 151 -AEVIALADACFRGIGLEGFRLEL 173
Cdd:pfam00587 81 lEDYIKLIDRVYSRLGLEVRVVRL 104
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
355-424 |
4.00e-10 |
|
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: 56.25 E-value: 4.00e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 355 NKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQHAVALDALVQELQ 424
Cdd:cd00738 25 NALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGESETLHVDELPEFLV 94
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
45-199 |
8.34e-08 |
|
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: 52.51 E-value: 8.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 45 GYEHIELPIFEETGLFARgvgesTDVVTKEMYTFADRGDRSVTLRPEGTAGVMRAVIEHnldRGQLPVKLSYAGPFFRYE 124
Cdd:cd00768 17 GFQEVETPIVEREPLLEK-----AGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSH---IRKLPLRLAEIGPAFRNE 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 740843628 125 RPQAG--RYRQLQQVGVEAIGVD--DPALDAEVIALADACFRGIGLEGFRLELTSLGDNTCRPEYRAKLqEFLFELPLD 199
Cdd:cd00768 89 GGRRGlrRVREFTQLEGEVFGEDgeEASEFEELIELTEELLRALGIKLDIVFVEKTPGEFSPGGAGPGF-EIEVDHPEG 166
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
73-167 |
4.94e-04 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 41.90 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 73 KEMYTFADRGDRSVTLRPEGTAGVMRAVIEHnLDRGQLPVKLSYAGPFFRYerPQAGRYrqlqQVGVEAIGVDDPaldAE 152
Cdd:PRK12293 58 KELIRFSDEKNHQISLRADSTLDVVRIVTKR-LGRSTEHKKWFYIQPVFRY--PSNEIY----QIGAELIGEEDL---SE 127
|
90
....*....|....*
gi 740843628 153 VIALADACFRGIGLE 167
Cdd:PRK12293 128 ILNIAAEIFEELELE 142
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
355-424 |
6.84e-04 |
|
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: 38.64 E-value: 6.84e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 355 NKLRQAGIRADMSYGGRGLKGAMKGADRAGARFALVLGESELAAGEVQLKDLESHEQHAVALDALVQELQ 424
Cdd:cd00860 22 KKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGSMSLDEFIEKLK 91
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
16-363 |
1.33e-03 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 40.72 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 16 PKGVPDYVPPVSREFEAVRNSFQHRARLAGYEHIELPIFEETGLFARGVGESTDVVTkemYTFADR-GDRSVTLRPEGTA 94
Cdd:PRK12421 10 PDGVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQT---FKLIDQlSGRLMGVRADITP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 95 GVMRavIEHNLDRGQLPVKLSYAGPFFRyERPQA-GRYRQLQQVGVEAIGVDDPALDAEVIALADACFRGIGLEGFRL-- 171
Cdd:PRK12421 87 QVAR--IDAHLLNREGVARLCYAGSVLH-TLPQGlFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGVPALHLdl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 172 ---------------------ELTSLGDNTCRPEyrakLQEFLFELPLDEETRHR----ANINP-LRVLDDKRPEMQEML 225
Cdd:PRK12421 164 ghvgifrrlaelaglspeeeeELFDLLQRKALPE----LAEVCQNLGVGSDLRRMfyalARLNGgLEALDRALSVLALQD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740843628 226 ADAPLMLDHLSDSArshfEAVTGLLDDMKVPYVINPrmVRGLDYYTKTCFEFVHDGLGAqsGIGGGGRYDGlMAQLGGQE 305
Cdd:PRK12421 240 AAIRQALDELKTLA----AHLKNRWPELPVSIDLAE--LRGYHYHTGLVFAAYIPGRGQ--ALARGGRYDG-IGEAFGRA 310
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 740843628 306 LSGIGFGLGVdRALLALeaegkQASDGRRVDVYGVALGEEAAHTmavQINKLRQAGIR 363
Cdd:PRK12421 311 RPATGFSMDL-KELLAL-----QFLEEEAGAILAPWGDDPDLLA---AIAELRQQGER 359
|
|
| |
