|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-418 |
0e+00 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 641.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 2 AKTIQAIRGMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEvtDVVEKEMYSFEDRNGDSLSLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 82 PEGTAGCVRSGIENGLLYNQEQRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdKHV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL-KDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 162 RLELNSIGSLEARAnyrTALIDYLE-----QHQEVLDEDAKRRMYTNPLR-VLDTKNPDIQAILGDAPKLSEYLDEESKQ 235
Cdd:COG0124 158 TLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 236 HFAGLCELLTAAGIEYQVNERLVRGLDYYNRTVFEWITESLGAQGTVCGGGRYDGLVEQLGGKATPAVGFAMGLERLVLM 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 316 METLELT-DVRRSVDVYMVSAGEGTMMAAMKLAEQLREQvpGLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAES 394
Cdd:COG0124 315 LEELGLLpAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420
....*....|....*....|....
gi 515611651 395 TVVLKDLIGGEQITISQTEVASKL 418
Cdd:COG0124 393 TVTLKDLATGEQETVPLDELVEYL 416
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-411 |
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: 627.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 6 QAIRGMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEVTDVVEKEMYSFEDRNGDSLSLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 86 AGCVRSGIENGLLYNQEQRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdKHVRLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL-KDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 166 NSIGSLEARANYRTALIDYLEQHQEVLDEDAKRRMYTNPLRVLDTKNPDIQAILGDAPKLSEYLDEESKQHFAGLCELLT 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 246 AAGIEYQVNERLVRGLDYYNRTVFEWITESLGAQGTVCGGGRYDGLVEQLGGKATPAVGFAMGLERLVLMMETLELTDVR 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 326 -RSVDVYMVSAGEGTMMAAMKLAEQLREQvpGLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAESTVVLKDLIGG 404
Cdd:TIGR00442 320 sKKPDVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
gi 515611651 405 EQITISQ 411
Cdd:TIGR00442 398 EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-421 |
1.52e-150 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 433.56 E-value: 1.52e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 1 MAKtIQAIRGMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEVTDVVEKEMYSFEDRNGDSLSL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 81 RPEGTAGCVRSGIENGLLY-NQEQRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdK 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQV-K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 160 HVRLELNSIGSLEARANYRTALIDYLEQHQEVLDEDAKRRMYTNPLRVLDTKNPDIQAILGDAPKLSEYLDEESKQHFAG 239
Cdd:CHL00201 159 NLILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 240 LCELLTAAGIEYQVNERLVRGLDYYNRTVFEWITESLGAQGTVCGGGRYDGLVEQLGGKATPAVGFAMGLERLVLMMETl 319
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKD- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 320 ELTDVRRSVDVYMVSAGEGTMMAAMKLAEQLREQVpgLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAESTVVLK 399
Cdd:CHL00201 318 NIILPKQSIDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIK 395
|
410 420
....*....|....*....|..
gi 515611651 400 DLIGGEQITISQTEVASKLTHL 421
Cdd:CHL00201 396 WLDEQVQENAQYSNFKQEISYL 417
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
21-317 |
2.43e-101 |
|
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: 301.83 E-value: 2.43e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 21 LWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRaigEVTDVVEKEMYSFEDRNGDSLSLRPEGTAGCVRSGIENGLLYN 100
Cdd:cd00773 4 LRRYIEDTLREVFERYGYEEIDTPVFEYTELFLR---KSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 101 QEQRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdKHVRLELNSIGSLEARANyrta 180
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL-KDFQIKINHRGILDGIAG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 181 lidyleqhqeVLDEDAKRRMytnplrvldtknpdiqailgdapKLSEYLDEESKQHFAGLCELLTAAG--IEYQVNERLV 258
Cdd:cd00773 156 ----------LLEDREEYIE-----------------------RLIDKLDKEALAHLEKLLDYLEALGvdIKYSIDLSLV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 515611651 259 RGLDYYNRTVFEWITESLGAQGTVCGGGRYDGLVEQLGGKATPAVGFAMGLERLVLMME 317
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 ... |
10-312 |
7.38e-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: 136.56 E-value: 7.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 10 GMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEmthlFSRAIGEVTDVVEKEMYSFEDRNGDSLSLRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLE----YLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 90 RsgIENGLLYNQE-QRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIDkHVRLELNSI 168
Cdd:pfam13393 77 R--IDAHRLNRPGpLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVP-GVTLDLGHV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 169 G-------SLEARANYRTALIDYLEQH-----QEVLDEDAKRRMYTNPLRVLDTKNPDIQAI------LGDAPKLSEYLD 230
Cdd:pfam13393 154 GlvralleAAGLSEALEEALRAALQRKdaaelAELAAEAGLPPALRRALLALPDLYGGPEVLdearaaLPGLPALQEALD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 231 EeskqhfagLCELLTAA-----GIEYQVNERLVRGLDYYNRTVFEWITEslGAQGTVCGGGRYDGLVEQLgGKATPAVGF 305
Cdd:pfam13393 234 E--------LEALAALLealgdGVRLTFDLAELRGYEYYTGIVFAAYAP--GVGEPLARGGRYDDLGAAF-GRARPATGF 302
|
....*..
gi 515611651 306 AMGLERL 312
Cdd:pfam13393 303 SLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-418 |
0e+00 |
|
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 439894 [Multi-domain] Cd Length: 422 Bit Score: 641.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 2 AKTIQAIRGMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEvtDVVEKEMYSFEDRNGDSLSLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 82 PEGTAGCVRSGIENGLLYNQEQRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdKHV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL-KDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 162 RLELNSIGSLEARAnyrTALIDYLE-----QHQEVLDEDAKRRMYTNPLR-VLDTKNPDIQAILGDAPKLSEYLDEESKQ 235
Cdd:COG0124 158 TLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 236 HFAGLCELLTAAGIEYQVNERLVRGLDYYNRTVFEWITESLGAQGTVCGGGRYDGLVEQLGGKATPAVGFAMGLERLVLM 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 316 METLELT-DVRRSVDVYMVSAGEGTMMAAMKLAEQLREQvpGLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAES 394
Cdd:COG0124 315 LEELGLLpAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420
....*....|....*....|....
gi 515611651 395 TVVLKDLIGGEQITISQTEVASKL 418
Cdd:COG0124 393 TVTLKDLATGEQETVPLDELVEYL 416
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-411 |
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: 627.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 6 QAIRGMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEVTDVVEKEMYSFEDRNGDSLSLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 86 AGCVRSGIENGLLYNQEQRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdKHVRLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL-KDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 166 NSIGSLEARANYRTALIDYLEQHQEVLDEDAKRRMYTNPLRVLDTKNPDIQAILGDAPKLSEYLDEESKQHFAGLCELLT 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 246 AAGIEYQVNERLVRGLDYYNRTVFEWITESLGAQGTVCGGGRYDGLVEQLGGKATPAVGFAMGLERLVLMMETLELTDVR 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 326 -RSVDVYMVSAGEGTMMAAMKLAEQLREQvpGLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAESTVVLKDLIGG 404
Cdd:TIGR00442 320 sKKPDVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
gi 515611651 405 EQITISQ 411
Cdd:TIGR00442 398 EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-421 |
1.52e-150 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 433.56 E-value: 1.52e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 1 MAKtIQAIRGMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEVTDVVEKEMYSFEDRNGDSLSL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 81 RPEGTAGCVRSGIENGLLY-NQEQRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdK 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQV-K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 160 HVRLELNSIGSLEARANYRTALIDYLEQHQEVLDEDAKRRMYTNPLRVLDTKNPDIQAILGDAPKLSEYLDEESKQHFAG 239
Cdd:CHL00201 159 NLILDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 240 LCELLTAAGIEYQVNERLVRGLDYYNRTVFEWITESLGAQGTVCGGGRYDGLVEQLGGKATPAVGFAMGLERLVLMMETl 319
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKD- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 320 ELTDVRRSVDVYMVSAGEGTMMAAMKLAEQLREQVpgLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAESTVVLK 399
Cdd:CHL00201 318 NIILPKQSIDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIK 395
|
410 420
....*....|....*....|..
gi 515611651 400 DLIGGEQITISQTEVASKLTHL 421
Cdd:CHL00201 396 WLDEQVQENAQYSNFKQEISYL 417
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
21-317 |
2.43e-101 |
|
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: 301.83 E-value: 2.43e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 21 LWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRaigEVTDVVEKEMYSFEDRNGDSLSLRPEGTAGCVRSGIENGLLYN 100
Cdd:cd00773 4 LRRYIEDTLREVFERYGYEEIDTPVFEYTELFLR---KSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 101 QEQRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdKHVRLELNSIGSLEARANyrta 180
Cdd:cd00773 81 LPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL-KDFQIKINHRGILDGIAG---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 181 lidyleqhqeVLDEDAKRRMytnplrvldtknpdiqailgdapKLSEYLDEESKQHFAGLCELLTAAG--IEYQVNERLV 258
Cdd:cd00773 156 ----------LLEDREEYIE-----------------------RLIDKLDKEALAHLEKLLDYLEALGvdIKYSIDLSLV 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 515611651 259 RGLDYYNRTVFEWITESLGAQGTVCGGGRYDGLVEQLGGKATPAVGFAMGLERLVLMME 317
Cdd:cd00773 203 RGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
13-317 |
2.40e-42 |
|
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: 151.23 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 13 DCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGevtdVVEKEMYSFEDRNGDSLSLRPEGTAGCVRsg 92
Cdd:TIGR00443 2 DLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSG----ILNEDLFKLFDQLGRVLGLRPDMTAPIAR-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 93 IENGLLYNQE--QRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdKHVRLEL----- 165
Cdd:TIGR00443 76 LVSTRLRDRPlpLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGL-KDFKIELghvgl 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 166 ------NSIGSLEARANYRTALIDY----LEQ---HQEVLDEDAKR-----RMYTNPLRVLDtknpDIQAILGDaPKLSE 227
Cdd:TIGR00443 155 vralleEAGLPEEAREALREALARKdlvaLEElvaELGLSPEVRERllalpRLRGDGEEVLE----EARALAGS-ETAEA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 228 YLDEESKqhfagLCELLTAAGIEYQVNERL--VRGLDYYNRTVFEWITESLGAqgTVCGGGRYDGLVEQLgGKATPAVGF 305
Cdd:TIGR00443 230 ALDELEA-----VLELLEARGVEEYISLDLglVRGYHYYTGLIFEGYAPGLGA--PLAGGGRYDELLGRF-GRPLPATGF 301
|
330
....*....|..
gi 515611651 306 AMGLERLVLMME 317
Cdd:TIGR00443 302 ALNLERLLEALT 313
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
10-359 |
2.75e-42 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 153.10 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 10 GMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGevtDVVEKEMYSFEDR-NGDSLSLRPEGTAGC 88
Cdd:PRK12292 8 GIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGG---AILDLRTFKLVDQlSGRTLGLRPDMTAQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 89 VRsgIENGLLYNQE--QRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIDKhVRLEL- 165
Cdd:PRK12292 85 AR--IAATRLANRPgpLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPN-FTLDLg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 166 ----------NSIGSLEARANYRTALI--DY--LEQHQEVLDEDAKRRMytnpLRVLDTKNPDiqAILGDAPKLseYLDE 231
Cdd:PRK12292 162 hvglfralleAAGLSEELEEVLRRALAnkDYvaLEELVLDLSEELRDAL----LALPRLRGGR--EVLEEARKL--LPSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 232 ESKQHFAGLCELLTAAGiEYQVNERL------VRGLDYYNRTVFEWITESLGAQgtVCGGGRYDGLVEQLgGKATPAVGF 305
Cdd:PRK12292 234 PIKRALDELEALAEALE-KYGYGIPLsldlglLRHLDYYTGIVFEGYVDGVGNP--IASGGRYDDLLGRF-GRARPATGF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 515611651 306 AMGLERLvlmMETLELTDVRRSVDVYMVSAGEGtMMAAMKLAEQLREQvpGLRV 359
Cdd:PRK12292 310 SLDLDRL---LELQLELPVEARKDLVIAPDSEA-LAAALAAAQELRKK--GEIV 357
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
30-409 |
1.13e-41 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 153.74 E-value: 1.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 30 KNVISAYGYNEVRMPIVEMTHLFSRAIGE-VTDvvekEMYSFEDRNGDSLSLRPEGTAGCVRSGIENGllynQEQRL--- 105
Cdd:PLN02530 95 REVSRLFGFEEVDAPVLESEELYIRKAGEeITD----QLYNFEDKGGRRVALRPELTPSLARLVLQKG----KSLSLplk 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 106 WY-MGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGI-DKHVRLELNSIGSLEARANYRT---- 179
Cdd:PLN02530 167 WFaIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGItSSDVGIKVSSRKVLQAVLKSYGipee 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 180 ------ALIDYLEQ--HQEV--------LDEDAKRRMytnpLRVLDTKN-PDIQAILGDApklSEYLDEeSKQHFAgLCE 242
Cdd:PLN02530 247 sfapvcVIVDKLEKlpREEIekeldtlgVSEEAIEGI----LDVLSLKSlDDLEALLGAD---SEAVAD-LKQLFS-LAE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 243 lltAAGIE--YQVNERLVRGLDYYNRTVFEWITESlGAQGTVCGGGRYDGLVEQLGGKATPAVGFAMGLERLV-LMMETL 319
Cdd:PLN02530 318 ---AYGYQdwLVFDASVVRGLAYYTGIVFEGFDRA-GKLRAICGGGRYDRLLSTFGGEDTPACGFGFGDAVIVeLLKEKG 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 320 ELTDVRRSVDVYMVSAGEGTMMAAMKLAEQLREQvpGLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAESTVVLK 399
Cdd:PLN02530 394 LLPELPHQVDDVVFALDEDLQGAAAGVASRLREK--GRSVDLVLEPKKLKWVFKHAERIGAKRLVLVGASEWERGMVRVK 471
|
410
....*....|
gi 515611651 400 DLIGGEQITI 409
Cdd:PLN02530 472 DLSSGEQTEV 481
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
6-414 |
3.61e-41 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 151.04 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 6 QAIRGMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEVTDVVeKEMYSFEDRNGDSLSLRPEGT 85
Cdd:PRK12420 5 RNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGDEIL-KEIYTLTDQGKRDLALRYDLT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 86 AGCVRSgiengLLYNQEQRLWY----MGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIDKHV 161
Cdd:PRK12420 84 IPFAKV-----VAMNPNIRLPFkryeIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLEVTI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 162 RLE--------LNSIGSLEARANYRTALIDYLEQ--HQEVLDEDAKRRMyTNPL--RVLDTKNPDIQAILGD-APKLSEY 228
Cdd:PRK12420 159 QYNnrkllngiLQAIGIPTELTSDVILSLDKIEKigIDGVRKDLLERGI-SEEMadTICNTVLSCLQLSIADfKEAFNNP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 229 LDEESKQHFAGLCELLTAAGIEYQV--NERLVRGLDYYNRTVFEWITESLGAQGTVCGGGRYDGLVEQLGGK--ATPAVG 304
Cdd:PRK12420 238 LVAEGVNELQQLQQYLIALGINENCifNPFLARGLTMYTGTVYEIFLKDGSITSSIGSGGRYDNIIGAFRGDdmNYPTVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 305 FAMGLERLVLMMETLELTDvrRSVDVYMVSAGegTMMAAMKLAEQLREQvPGLRVMNHFGGGNFKKQFKRADKVGAAVAL 384
Cdd:PRK12420 318 ISFGLDVIYTALSQKETIS--STADVFIIPLG--TELQCLQIAQQLRST-TGLKVELELAGRKLKKALNYANKENIPYVL 392
|
410 420 430
....*....|....*....|....*....|
gi 515611651 385 VLGEDEVAESTVVLKDLIGGEQITISQTEV 414
Cdd:PRK12420 393 IIGEEEVSTGTVMLRNMKEGSEVKVPLSSL 422
|
|
| 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 ... |
21-317 |
2.33e-38 |
|
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: 138.29 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 21 LWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIgeVTDVVEKEMYSFEDRN----GDSLSLRPEGTAGCVRSGIENG 96
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG--HLDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFSGEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 97 LLY-NQEQRLWYMGPMFRHERPQ---KGRYRQFHQCGVEVFGLDG--PDVDAELIMMTARLWRELGIdkHVRLELNSIGS 170
Cdd:cd00670 82 LSYrALPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGEPEeaEEERREWLELAEEIARELGL--PVRVVVADDPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 171 LEARANyrtalidyleqhqevldedakrrmytnplrvldtknpdiqailgdapklseyldeeskqhfaglcelltaagie 250
Cdd:cd00670 160 FGRGGK-------------------------------------------------------------------------- 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515611651 251 yqvnerlvRGLDYYNRTVFEW--ITESLGAQGTVCGGGRYDGLVEQ---------LGGKATPAVGFAMGLERLVLMME 317
Cdd:cd00670 166 --------RGLDAGRETVVEFelLLPLPGRAKETAVGSANVHLDHFgasfkidedGGGRAHTGCGGAGGEERLVLALL 235
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
15-317 |
6.03e-38 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 139.54 E-value: 6.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 15 LPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEVTDvveKEMYSFEDRNGDSLSLRPEGTAGCVRsgIE 94
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVAR--IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 95 NGLLYNQE--QRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdKHVRLELNSIG--- 169
Cdd:COG3705 76 ATRLANRPgpLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGL-EDFTLDLGHVGlfr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 170 ----SLEARANYRTALIDYLEQ----------HQEVLDEDAKRRMY-----TNPLRVLDtknpDIQAILGDApKLSEYLD 230
Cdd:COG3705 155 alleALGLSEEQREELRRALARkdaveleellAELGLSEELAEALLalpelYGGEEVLA----RARALLLDA-AIRAALD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 231 EeskqhFAGLCELLTAAGIEyqvnERL------VRGLDYYNRTVFEWITESLGaqGTVCGGGRYDGLVEQLGgKATPAVG 304
Cdd:COG3705 230 E-----LEALAEALAARGPD----VRLtfdlseLRGYDYYTGIVFEAYAPGVG--DPLARGGRYDGLLAAFG-RARPATG 297
|
330
....*....|...
gi 515611651 305 FAMGLERLVLMME 317
Cdd:COG3705 298 FSLDLDRLLRALP 310
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
7.38e-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: 136.56 E-value: 7.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 10 GMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEmthlFSRAIGEVTDVVEKEMYSFEDRNGDSLSLRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLE----YLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 90 RsgIENGLLYNQE-QRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIDkHVRLELNSI 168
Cdd:pfam13393 77 R--IDAHRLNRPGpLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVP-GVTLDLGHV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 169 G-------SLEARANYRTALIDYLEQH-----QEVLDEDAKRRMYTNPLRVLDTKNPDIQAI------LGDAPKLSEYLD 230
Cdd:pfam13393 154 GlvralleAAGLSEALEEALRAALQRKdaaelAELAAEAGLPPALRRALLALPDLYGGPEVLdearaaLPGLPALQEALD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 231 EeskqhfagLCELLTAA-----GIEYQVNERLVRGLDYYNRTVFEWITEslGAQGTVCGGGRYDGLVEQLgGKATPAVGF 305
Cdd:pfam13393 234 E--------LEALAALLealgdGVRLTFDLAELRGYEYYTGIVFAAYAP--GVGEPLARGGRYDDLGAAF-GRARPATGF 302
|
....*..
gi 515611651 306 AMGLERL 312
Cdd:pfam13393 303 SLDLEAL 309
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
9-418 |
1.32e-31 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 127.31 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 9 RGMNDCLPTQSPLWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEVTdvveKEMYSFEDRNGDSLSLRPEGTAGC 88
Cdd:PLN02972 331 KGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDS----KLIYDLADQGGELCSLRYDLTVPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 89 VRSGIENGLlynQEQRLWYMGPMFRHERPQKGRYRQFHQCGVEVFGLDGPDV-DAELIMMTARLWRELGIDKHvRLELNS 167
Cdd:PLN02972 407 ARYVAMNGI---TSFKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPMGpDFEIIKVLTELLDELDIGTY-EVKLNH 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 168 IGSLEAR--------ANYRT--ALIDYLEQH------QEVLDEDAKRRMYTNPL-RVLDTKNPDIQAILGDAPKLSEYLD 230
Cdd:PLN02972 483 RKLLDGMleicgvppEKFRTicSSIDKLDKQsfeqvkKEMVEEKGLSNETADKIgNFVKERGPPLELLSKLRQEGSEFLG 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 231 EESKQ----HFAGLCELLTAAGIEYQV--NERLVRGLDYYNRTVFEWITEslGAQ-GTVCGGGRYDGLVEQLGGKATPAV 303
Cdd:PLN02972 563 NASSRaaldELEIMFKALEKSKAIGKIvfDLSLARGLDYYTGVIYEAVFK--GAQvGSIAAGGRYDNLVGMFSGKQVPAV 640
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 304 GFAMGLERLVLMMETLEL--TDVRRSVD--VYMVSAGEGTMMAAMKLAEQL------REQVPGLRVMNHfgggnfkkqFK 373
Cdd:PLN02972 641 GVSLGIERVFAIMEQQEEekSQVIRPTEteVLVSIIGDDKLALAAELVSELwnagikAEYKVSTRKAKH---------LK 711
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 515611651 374 RADKVGAAVALVLGEDEVAESTVVLKDLIGGEQITISQTEVASKL 418
Cdd:PLN02972 712 RAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQEL 756
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
327-418 |
5.96e-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: 113.79 E-value: 5.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 327 SVDVYMVSAGEGTMMAAMKLAEQLREQvpGLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAESTVVLKDLIGGEQ 406
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDA--GIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQ 78
|
90
....*....|..
gi 515611651 407 ITISQTEVASKL 418
Cdd:cd00859 79 ETVALDELVEEL 90
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
21-173 |
1.39e-29 |
|
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: 114.14 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 21 LWQKVEGTVKNVISAYGYNEVRMPIVEMTHLFSRAIGEvtdvvEKEMYSFEDRNGDSLSLRPEGTAGCVRSGIENglLYN 100
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE-----PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSH--IRK 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515611651 101 QEQRLWYMGPMFRHERPQKG--RYRQFHQCGVEVFGLDGPDVD--AELIMMTARLWRELGIDKHVRLELNSIGSLEA 173
Cdd:cd00768 74 LPLRLAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGEDGEEASefEELIELTEELLRALGIKLDIVFVEKTPGEFSP 150
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
68-173 |
3.66e-24 |
|
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: 98.64 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 68 YSFEDRNGDSLSLRPEGTAGCVRSGIENGL-LYNQEQRLWYMGPMFRHERP--QKG--RYRQFHQCGVEVFGLDG--PDV 140
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLrSKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHAPGqsPDE 80
|
90 100 110
....*....|....*....|....*....|...
gi 515611651 141 DAELIMMTARLWRELGIDKHVRLELNSIGSLEA 173
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGSAFY 113
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
65-312 |
5.38e-20 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 90.76 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 65 KEMYSFEDRNGDSLSLRPEGTAGCVRSGIENGLlyNQEQRLWYMGPMFRHerpQKGRYRQFHQCGVEVFG-LDGPDVDAE 143
Cdd:PRK12295 47 RRIFVTSDENGEELCLRPDFTIPVCRRHIATAG--GEPARYAYLGEVFRQ---RRDRASEFLQAGIESFGrADPAAADAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 144 LIMMTARLWRELGIDKhVRLELNSIGSLEA--------------------RANYRTALIDYL--------EQHQEVL--- 192
Cdd:PRK12295 122 VLALALEALAALGPGD-LEVRLGDVGLFAAlvdalglppgwkrrllrhfgRPRSLDALLARLagprvdplDEHAGVLaal 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 193 -DEDAKRRMYTNPL-----------------RVLDTK-------------------------NPD-----IQAILGDAP- 223
Cdd:PRK12295 201 aDEAAARALVEDLMsiagispvggrspaeiaRRLLEKaalaaaarlpaealavlerflaisgPPDaalaaLRALAADAGl 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 224 KLSEYLDEeskqhFAGLCELLTAAGIEYqvnERLV------RGLDYYNRTVFEWITESLGAqGTVCGGGRYDGLVEQLG- 296
Cdd:PRK12295 281 DLDAALDR-----FEARLAALAARGIDL---ERLRfsasfgRPLDYYTGFVFEIRAAGNGD-PPLAGGGRYDGLLTRLGa 351
|
330
....*....|....*.
gi 515611651 297 GKATPAVGFAMGLERL 312
Cdd:PRK12295 352 GEPIPAVGFSIWLDRL 367
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
329-418 |
2.77e-12 |
|
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: 62.60 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 329 DVYMVSAGEGT---MMAAMKLAEQLREQvpGLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAESTVVLKDLIGGE 405
Cdd:pfam03129 1 QVVVIPLGEKAeelEEYAQKLAEELRAA--GIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGE 78
|
90
....*....|...
gi 515611651 406 QITISQTEVASKL 418
Cdd:pfam03129 79 QETVSLDELVEKL 91
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
328-418 |
1.24e-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: 57.79 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 328 VDVYMVSAGEGTMMA---AMKLAEQLREQvpGLRVMNHFGGGNFKKQFKRADKVGAAVALVLGEDEVAESTVVLKDLIGG 404
Cdd:cd00738 2 IDVAIVPLTDPRVEAreyAQKLLNALLAN--GIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....
gi 515611651 405 EQITISQTEVASKL 418
Cdd:cd00738 80 ESETLHVDELPEFL 93
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
104-365 |
7.79e-09 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 57.29 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 104 RLWYMGPMFrHERPQK-GRYRQFHQCGVEVFGLDGPDVDAELIMMTARLWRELGIdKHVRLELNSIG---SLEARA---- 175
Cdd:PRK12421 103 RLCYAGSVL-HTLPQGlFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGV-PALHLDLGHVGifrRLAELAglsp 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 176 NYRTALIDYLEQH-----QEVLDEDAKRRMYTNPLRVLDTKNPDIQAILGDAPKLSEYlDEESKQHFAGLCELLTAAG-- 248
Cdd:PRK12421 181 EEEEELFDLLQRKalpelAEVCQNLGVGSDLRRMFYALARLNGGLEALDRALSVLALQ-DAAIRQALDELKTLAAHLKnr 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 249 -----IEYQVNErlVRGLDYYNRTVFEWITESLGAQgtVCGGGRYDGlVEQLGGKATPAVGFAMGLERLVLMMETLEltd 323
Cdd:PRK12421 260 wpelpVSIDLAE--LRGYHYHTGLVFAAYIPGRGQA--LARGGRYDG-IGEAFGRARPATGFSMDLKELLALQFLEE--- 331
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 515611651 324 vrrsvDVYMVSAGEGTMMAAMKLAEQLREQvpGLRVMNHFGG 365
Cdd:PRK12421 332 -----EAGAILAPWGDDPDLLAAIAELRQQ--GERVVQLLPG 366
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
64-307 |
1.01e-06 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 49.99 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 64 EKEMYSFEDRNGDSLSLRPEGTAGCVRSgIENGLLYNQEQRLW-YMGPMFRHerPQkgryRQFHQCGVEVfgLDGPDVdA 142
Cdd:PRK12293 57 EKELIRFSDEKNHQISLRADSTLDVVRI-VTKRLGRSTEHKKWfYIQPVFRY--PS----NEIYQIGAEL--IGEEDL-S 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 143 ELIMMTARLWRELGIDKHvrLELNSIGSLEARANYRTALIDYLEqHQEVLDEDAKRRMYTNPLRVLDTKNpDIQAILGDA 222
Cdd:PRK12293 127 EILNIAAEIFEELELEPI--LQISNIKIPKLVAEILGLDIEVFK-KGQIEKLLAQNVPWLNKLVRIKTLE-DLDEVIELV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515611651 223 P-KLSEYLDEeskqhfagLCELltAAGIEYqvnERLV------RGLDYYNRTVFEWITESLgaqgTVCGGGRY--DGLve 293
Cdd:PRK12293 203 PdEIKEELEK--------LKEL--AESIKY---ENLViaplyyAKMRYYDDLFFRFFDGNS----TLASGGNYeiDGI-- 263
|
250
....*....|....
gi 515611651 294 qlggkatPAVGFAM 307
Cdd:PRK12293 264 -------SSSGFAL 270
|
|
| |
