|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-407 |
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: 561.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 1 MSITAVKGFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGEttDIVEKEMYSFLDRHGDGLTLRP 80
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 81 EGTASVVRAYIEHKLYTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITL 160
Cdd:COG0124 80 EGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 161 YINSLGCAECRPgykQTLTRYLE-----GVKDRLCENCQRRLSVNPLRA-LDCKSTGCIAATQDAPKITDSLCTRCKQHF 234
Cdd:COG0124 160 EINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRAiLDSKGPDCQEVLADAPKLLDYLGEEGLAHF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 235 IFVTDSLSRRGIIAIPNPRMVRGLDYYTKTTFEITaAAGLGAQNAVAAGGRYDGLVKDLGGPATPCFGFAMGMERVALLL 314
Cdd:COG0124 237 EEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIV-TDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 315 QETGLRSVKEPPLCAFIA-LGKEAEMAGTAIIKILREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVI 393
Cdd:COG0124 316 EELGLLPAAEPPPDVYVVpLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANGTVT 395
|
410
....*....|....
gi 1084827069 394 IKDMKTATQDTINL 407
Cdd:COG0124 396 LKDLATGEQETVPL 409
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
5-407 |
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: 547.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 5 AVKGFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGETTDIVEKEMYSFLDRHGDGLTLRPEGTA 84
Cdd:TIGR00442 2 KPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 85 SVVRAYIEHKLYTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLYINS 164
Cdd:TIGR00442 82 PVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTLEINS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 165 LGCAECRPGYKQTLTRYLEGVKDRLCENCQRRLSVNPLRALDCKSTGCIAATQDAPKITDSLCTRCKQHFIFVTDSLSRR 244
Cdd:TIGR00442 162 LGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLDAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 245 GIIAIPNPRMVRGLDYYTKTTFEITaAAGLGAQNAVAAGGRYDGLVKDLGGPATPCFGFAMGMERVALLLQETGLRSVKE 324
Cdd:TIGR00442 242 GIPYKIDPSLVRGLDYYTGTVFEFV-TDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPPS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 325 PPLCAFIA-LGKEAEMAGTAIIKILREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVIIKDMKTATQD 403
Cdd:TIGR00442 321 KKPDVYVVpLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQE 400
|
....
gi 1084827069 404 TINL 407
Cdd:TIGR00442 401 TVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
3-409 |
5.72e-117 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 348.04 E-value: 5.72e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 3 ITAVKGFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGETTDIVEKEMYSFLDRHGDGLTLRPEG 82
Cdd:CHL00201 4 IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLRPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 83 TASVVRAYIEHKL-YTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLY 161
Cdd:CHL00201 84 TAGIVRAFIENKMdYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKNLILD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 162 INSLGCAECRPGYKQTLTRYLEGVKDRLCENCQRRLSVNPLRALDCKSTGCIAATQDAPKITDSLCTRCKQHFIFVTDSL 241
Cdd:CHL00201 164 INSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYDVCTYL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 242 SRRGIIAIPNPRMVRGLDYYTKTTFEITAAAGLGaQNAVAAGGRYDGLVKDLGGPATPCFGFAMGMERVaLLLQETGLRS 321
Cdd:CHL00201 244 NLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNG-QDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERL-LLIAKDNIIL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 322 VKEPPLCAFIALGKEAEMAGTAIIKILREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVIIKDMKTAT 401
Cdd:CHL00201 322 PKQSIDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQV 401
|
....*...
gi 1084827069 402 QDTINLLD 409
Cdd:CHL00201 402 QENAQYSN 409
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
16-315 |
2.81e-89 |
|
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: 271.01 E-value: 2.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 16 ETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGettDIVEKEMYSFLDRHGDGLTLRPEGTASVVRAYIEHKL 95
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSG---DEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 96 YTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLYINSLG-------CA 168
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGildgiagLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 169 ECRPGYKQTLTRYLEgvkdrlcencqrRLSVNPLRALDckstgciaatqdapKITDSLctRCKQHFIFvtdslsrrgiia 248
Cdd:cd00773 158 EDREEYIERLIDKLD------------KEALAHLEKLL--------------DYLEAL--GVDIKYSI------------ 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084827069 249 ipNPRMVRGLDYYTKTTFEITaAAGLGAQNAVAAGGRYDGLVKDLGGPATPCFGFAMGMERVALLLQ 315
Cdd:cd00773 198 --DLSLVRGLDYYTGIVFEAV-ADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-310 |
1.13e-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: 138.49 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 8 GFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEktelFMRSIGETTDIVEKEMYSFLDRHGDGLTLRPEGTASVV 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLE----YLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 88 RAYiEHKLYTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLYINSLGC 167
Cdd:pfam13393 77 RID-AHRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 168 -------AECRPGYKQTLTRYLEGvKDRL-CENCQRRLSVNP-LRALDCKSTGCI-------AATQDAPkiTDSLCTRCK 231
Cdd:pfam13393 156 vralleaAGLSEALEEALRAALQR-KDAAeLAELAAEAGLPPaLRRALLALPDLYggpevldEARAALP--GLPALQEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 232 QHFIFVTDSLSRRGiIAIP---NPRMVRGLDYYTKTTFEITAAaglGAQNAVAAGGRYDGLVKDLGGPAtPCFGFAMGME 308
Cdd:pfam13393 233 DELEALAALLEALG-DGVRltfDLAELRGYEYYTGIVFAAYAP---GVGEPLARGGRYDDLGAAFGRAR-PATGFSLDLE 307
|
..
gi 1084827069 309 RV 310
Cdd:pfam13393 308 AL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-407 |
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: 561.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 1 MSITAVKGFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGEttDIVEKEMYSFLDRHGDGLTLRP 80
Cdd:COG0124 2 MKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLRP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 81 EGTASVVRAYIEHKLYTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITL 160
Cdd:COG0124 80 EGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDFTL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 161 YINSLGCAECRPgykQTLTRYLE-----GVKDRLCENCQRRLSVNPLRA-LDCKSTGCIAATQDAPKITDSLCTRCKQHF 234
Cdd:COG0124 160 EINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRAiLDSKGPDCQEVLADAPKLLDYLGEEGLAHF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 235 IFVTDSLSRRGIIAIPNPRMVRGLDYYTKTTFEITaAAGLGAQNAVAAGGRYDGLVKDLGGPATPCFGFAMGMERVALLL 314
Cdd:COG0124 237 EEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIV-TDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 315 QETGLRSVKEPPLCAFIA-LGKEAEMAGTAIIKILREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVI 393
Cdd:COG0124 316 EELGLLPAAEPPPDVYVVpLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANGTVT 395
|
410
....*....|....
gi 1084827069 394 IKDMKTATQDTINL 407
Cdd:COG0124 396 LKDLATGEQETVPL 409
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
5-407 |
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: 547.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 5 AVKGFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGETTDIVEKEMYSFLDRHGDGLTLRPEGTA 84
Cdd:TIGR00442 2 KPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGTA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 85 SVVRAYIEHKLYTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLYINS 164
Cdd:TIGR00442 82 PVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTLEINS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 165 LGCAECRPGYKQTLTRYLEGVKDRLCENCQRRLSVNPLRALDCKSTGCIAATQDAPKITDSLCTRCKQHFIFVTDSLSRR 244
Cdd:TIGR00442 162 LGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLDAL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 245 GIIAIPNPRMVRGLDYYTKTTFEITaAAGLGAQNAVAAGGRYDGLVKDLGGPATPCFGFAMGMERVALLLQETGLRSVKE 324
Cdd:TIGR00442 242 GIPYKIDPSLVRGLDYYTGTVFEFV-TDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPPS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 325 PPLCAFIA-LGKEAEMAGTAIIKILREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVIIKDMKTATQD 403
Cdd:TIGR00442 321 KKPDVYVVpLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETGEQE 400
|
....
gi 1084827069 404 TINL 407
Cdd:TIGR00442 401 TVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
3-409 |
5.72e-117 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 348.04 E-value: 5.72e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 3 ITAVKGFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGETTDIVEKEMYSFLDRHGDGLTLRPEG 82
Cdd:CHL00201 4 IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLRPEG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 83 TASVVRAYIEHKL-YTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLY 161
Cdd:CHL00201 84 TAGIVRAFIENKMdYHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKNLILD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 162 INSLGCAECRPGYKQTLTRYLEGVKDRLCENCQRRLSVNPLRALDCKSTGCIAATQDAPKITDSLCTRCKQHFIFVTDSL 241
Cdd:CHL00201 164 INSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYDVCTYL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 242 SRRGIIAIPNPRMVRGLDYYTKTTFEITAAAGLGaQNAVAAGGRYDGLVKDLGGPATPCFGFAMGMERVaLLLQETGLRS 321
Cdd:CHL00201 244 NLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNG-QDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERL-LLIAKDNIIL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 322 VKEPPLCAFIALGKEAEMAGTAIIKILREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVIIKDMKTAT 401
Cdd:CHL00201 322 PKQSIDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQV 401
|
....*...
gi 1084827069 402 QDTINLLD 409
Cdd:CHL00201 402 QENAQYSN 409
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
16-315 |
2.81e-89 |
|
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: 271.01 E-value: 2.81e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 16 ETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGettDIVEKEMYSFLDRHGDGLTLRPEGTASVVRAYIEHKL 95
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSG---DEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 96 YTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLYINSLG-------CA 168
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGildgiagLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 169 ECRPGYKQTLTRYLEgvkdrlcencqrRLSVNPLRALDckstgciaatqdapKITDSLctRCKQHFIFvtdslsrrgiia 248
Cdd:cd00773 158 EDREEYIERLIDKLD------------KEALAHLEKLL--------------DYLEAL--GVDIKYSI------------ 197
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084827069 249 ipNPRMVRGLDYYTKTTFEITaAAGLGAQNAVAAGGRYDGLVKDLGGPATPCFGFAMGMERVALLLQ 315
Cdd:cd00773 198 --DLSLVRGLDYYTGIVFEAV-ADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
11-315 |
4.44e-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: 150.46 E-value: 4.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 11 DILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGettdIVEKEMYSFLDRHGDGLTLRPEGTASVVRAY 90
Cdd:TIGR00443 2 DLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSG----ILNEDLFKLFDQLGRVLGLRPDMTAPIARLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 91 IEHKLYTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLYI-------- 162
Cdd:TIGR00443 78 STRLRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELghvglvra 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 163 ---NSLGCAECRPGYKQTLTRY-LEGVKDRLCENCQRRLSVNPLRAL-DCKSTGcIAATQDAPKITDSlcTRCKQ---HF 234
Cdd:TIGR00443 158 lleEAGLPEEAREALREALARKdLVALEELVAELGLSPEVRERLLALpRLRGDG-EEVLEEARALAGS--ETAEAaldEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 235 IFVTDSLSRRGI---IAIpNPRMVRGLDYYTKTTFEITaAAGLGAqnAVAAGGRYDGLVKDLGGPAtPCFGFAMGMERVA 311
Cdd:TIGR00443 235 EAVLELLEARGVeeyISL-DLGLVRGYHYYTGLIFEGY-APGLGA--PLAGGGRYDELLGRFGRPL-PATGFALNLERLL 309
|
....
gi 1084827069 312 LLLQ 315
Cdd:TIGR00443 310 EALT 313
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
32-409 |
5.65e-41 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 151.43 E-value: 5.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 32 TSYGYSEIKVPVVEKTELFMRSIGETtdiVEKEMYSFLDRHGDGLTLRPEGTASVVRAYIEHKLYTAPINKLFYYGPMFR 111
Cdd:PLN02530 99 RLFGFEEVDAPVLESEELYIRKAGEE---ITDQLYNFEDKGGRRVALRPELTPSLARLVLQKGKSLSLPLKWFAIGQCWR 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 112 YERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQG--ITLYINSlgcaecRPGYKQTLTRYleGVKD-- 187
Cdd:PLN02530 176 YERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGITSsdVGIKVSS------RKVLQAVLKSY--GIPEes 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 188 --RLC-----------ENCQRRLSV---------NPLRALDCKSTGCIAAT--QDAPKITDslctrCKQHFIFVTDSLSR 243
Cdd:PLN02530 248 faPVCvivdkleklprEEIEKELDTlgvseeaieGILDVLSLKSLDDLEALlgADSEAVAD-----LKQLFSLAEAYGYQ 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 244 RGIIAipNPRMVRGLDYYTKTTFEITAAAGlgAQNAVAAGGRYDGLVKDLGGPATPCFGFAMGMERVALLLQETGLrsVK 323
Cdd:PLN02530 323 DWLVF--DASVVRGLAYYTGIVFEGFDRAG--KLRAICGGGRYDRLLSTFGGEDTPACGFGFGDAVIVELLKEKGL--LP 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 324 EPPLCA---FIALGKEAEMAGTAIIKILREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVIIKDMKTA 400
Cdd:PLN02530 397 ELPHQVddvVFALDEDLQGAAAGVASRLREKGRSVDLVLEPKKLKWVFKHAERIGAKRLVLVGASEWERGMVRVKDLSSG 476
|
....*....
gi 1084827069 401 TQDTINLLD 409
Cdd:PLN02530 477 EQTEVKLDE 485
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
23-314 |
2.00e-39 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 143.39 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 23 IEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGETTDiveKEMYSFLDRHGDGLTLRPEGTASVVRAYIeHKLYTAP-IN 101
Cdd:COG3705 11 LRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVARIAA-TRLANRPgPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 102 KLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITL------YINSL-GCAECRPGY 174
Cdd:COG3705 87 RLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLdlghvgLFRALlEALGLSEEQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 175 KQTLTRYLEGvKDRL-CENCQRRLSVNP---------------------LRALDcKSTGCIAATQDAPKITDSLCTRCKQ 232
Cdd:COG3705 167 REELRRALAR-KDAVeLEELLAELGLSEelaeallalpelyggeevlarARALL-LDAAIRAALDELEALAEALAARGPD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 233 HFIFVtdslsrrgiiaipNPRMVRGLDYYTKTTFEITAAaglGAQNAVAAGGRYDGLVKDLGG--PATpcfGFAMGMERV 310
Cdd:COG3705 245 VRLTF-------------DLSELRGYDYYTGIVFEAYAP---GVGDPLARGGRYDGLLAAFGRarPAT---GFSLDLDRL 305
|
....
gi 1084827069 311 ALLL 314
Cdd:COG3705 306 LRAL 309
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
8-310 |
1.13e-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: 138.49 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 8 GFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEktelFMRSIGETTDIVEKEMYSFLDRHGDGLTLRPEGTASVV 87
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLE----YLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 88 RAYiEHKLYTAPINKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLYINSLGC 167
Cdd:pfam13393 77 RID-AHRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 168 -------AECRPGYKQTLTRYLEGvKDRL-CENCQRRLSVNP-LRALDCKSTGCI-------AATQDAPkiTDSLCTRCK 231
Cdd:pfam13393 156 vralleaAGLSEALEEALRAALQR-KDAAeLAELAAEAGLPPaLRRALLALPDLYggpevldEARAALP--GLPALQEAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 232 QHFIFVTDSLSRRGiIAIP---NPRMVRGLDYYTKTTFEITAAaglGAQNAVAAGGRYDGLVKDLGGPAtPCFGFAMGME 308
Cdd:pfam13393 233 DELEALAALLEALG-DGVRltfDLAELRGYEYYTGIVFAAYAP---GVGEPLARGGRYDDLGAAFGRAR-PATGFSLDLE 307
|
..
gi 1084827069 309 RV 310
Cdd:pfam13393 308 AL 309
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
8-356 |
3.40e-37 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 139.23 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 8 GFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGETTDIvekEMYSFLDR-HGDGLTLRPEGTASV 86
Cdd:PRK12292 8 GIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDL---RTFKLVDQlSGRTLGLRPDMTAQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 87 VRAyIEHKLYTAPIN-KLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLYINSL 165
Cdd:PRK12292 85 ARI-AATRLANRPGPlRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDLGHV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 166 GCAEC-------RPGYKQTLTRYLEGvKDR---------LCENCQRRLsvnpLRALDCKstGCIAATQDAPKITDSL-CT 228
Cdd:PRK12292 164 GLFRAlleaaglSEELEEVLRRALAN-KDYvaleelvldLSEELRDAL----LALPRLR--GGREVLEEARKLLPSLpIK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 229 RCKQHFIFVTDSLSRRGiIAIP---NPRMVRGLDYYTKTTFEITAAaglGAQNAVAAGGRYDGLVKDLGG--PATpcfGF 303
Cdd:PRK12292 237 RALDELEALAEALEKYG-YGIPlslDLGLLRHLDYYTGIVFEGYVD---GVGNPIASGGRYDDLLGRFGRarPAT---GF 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1084827069 304 AMGMERVALLLQETglRSVKEPPLCafIALGKEAEMAGTAIIKILREDGLRVV 356
Cdd:PRK12292 310 SLDLDRLLELQLEL--PVEARKDLV--IAPDSEALAAALAAAQELRKKGEIVV 358
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
6-407 |
1.03e-36 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 138.71 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 6 VKGFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGETTDIVeKEMYSFLDRHGDGLTLRPEGT-- 83
Cdd:PRK12420 7 VKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGDEIL-KEIYTLTDQGKRDLALRYDLTip 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 84 -ASVV----RAYIEHKLYTapINKLFYYGPMfryerpQKGRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQgI 158
Cdd:PRK12420 86 fAKVVamnpNIRLPFKRYE--IGKVFRDGPI------KQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLE-V 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 159 TLYIN----------SLGC-AECRPGYKQTLTRY----LEGVKDRLCE-NCQRRLSVNPLRALDCKSTGCIAATQDAPki 222
Cdd:PRK12420 157 TIQYNnrkllngilqAIGIpTELTSDVILSLDKIekigIDGVRKDLLErGISEEMADTICNTVLSCLQLSIADFKEAF-- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 223 TDSLCTRCKQHFIFVTDSLSRRGI--IAIPNPRMVRGLDYYTKTTFEITAAAGLgAQNAVAAGGRYDGLVKDLGGP--AT 298
Cdd:PRK12420 235 NNPLVAEGVNELQQLQQYLIALGIneNCIFNPFLARGLTMYTGTVYEIFLKDGS-ITSSIGSGGRYDNIIGAFRGDdmNY 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 299 PCFGFAMGMERVALLLQEtglRSVKEP-PLCAFIALGKEAEMAGTAIiKILREDGLRVVEVFTEGGLKTRMKMADRLGAG 377
Cdd:PRK12420 314 PTVGISFGLDVIYTALSQ---KETISStADVFIIPLGTELQCLQIAQ-QLRSTTGLKVELELAGRKLKKALNYANKENIP 389
|
410 420 430
....*....|....*....|....*....|
gi 1084827069 378 FAIILGEDELKTGKVIIKDMKTATQDTINL 407
Cdd:PRK12420 390 YVLIIGEEEVSTGTVMLRNMKEGSEVKVPL 419
|
|
| 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 ... |
19-166 |
3.13e-26 |
|
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: 105.55 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 19 IWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIgeTTDIVEKEMYSFLDR----HGDGLTLRPEGTASVVRAYIEH- 93
Cdd:cd00670 4 LWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG--HLDGYRKEMYTFEDKgrelRDTDLVLRPAACEPIYQIFSGEi 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084827069 94 KLYTAPINKLFYYGPMFRYERPQ---KGRYRQFYQIGAEVMGEDH--PFMDAETIEMLVEFFKEIGLQgITLYINSLG 166
Cdd:cd00670 82 LSYRALPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGEPEeaEEERREWLELAEEIARELGLP-VRVVVADDP 158
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
7-402 |
3.86e-20 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 93.03 E-value: 3.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 7 KGFNDILPnetfiwkfiEQTACR---------IFTSYGYSEIKVPVVEKTELFMRSIGETTDIVekemYSFLDRHGDGLT 77
Cdd:PLN02972 331 KGTRDFAK---------EQMAIRekafsiitsVFKRHGATALDTPVFELRETLMGKYGEDSKLI----YDLADQGGELCS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 78 LRPEGTASVVRAYIEHKLYTApinKLFYYGPMFRYERPQKGRYRQFYQIGAEVMGEDHPFM-DAETIEMLVEFFKEIGLQ 156
Cdd:PLN02972 398 LRYDLTVPFARYVAMNGITSF---KRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPMGpDFEIIKVLTELLDELDIG 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 157 GITLYINSLG-------------------CAECRPGYKQTLtrylEGVKDRLCEncQRRLSVNPLRALdckstGCIAATQ 217
Cdd:PLN02972 475 TYEVKLNHRKlldgmleicgvppekfrtiCSSIDKLDKQSF----EQVKKEMVE--EKGLSNETADKI-----GNFVKER 543
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 218 DAPKitDSLCTRCKQHFIFVTDSLSRRGI--IAIP---------------NPRMVRGLDYYTKTTFEitaAAGLGAQ-NA 279
Cdd:PLN02972 544 GPPL--ELLSKLRQEGSEFLGNASSRAALdeLEIMfkalekskaigkivfDLSLARGLDYYTGVIYE---AVFKGAQvGS 618
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 280 VAAGGRYDGLVKDLGGPATPCFGFAMGMERVALLLQE------TGLRSVKEPPLCAFIALGKEAEMAGtaIIKILREDGL 353
Cdd:PLN02972 619 IAAGGRYDNLVGMFSGKQVPAVGVSLGIERVFAIMEQqeeeksQVIRPTETEVLVSIIGDDKLALAAE--LVSELWNAGI 696
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1084827069 354 RvvevfTEGGLKTRM----KMADRLGAGFAIILGEDELKTGKVIIKDMKTATQ 402
Cdd:PLN02972 697 K-----AEYKVSTRKakhlKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVE 744
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
19-174 |
1.43e-18 |
|
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: 83.71 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 19 IWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGEttdivEKEMYSFLDRHGDGLTLRPEGTASVVRAYIEHkLYTA 98
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE-----PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSH-IRKL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 99 PiNKLFYYGPMFRYERPQKG--RYRQFYQIGAEVMGED--HPFMDAETIEMLVEFFKEIGLQ-GITLYIN---SLGCAEC 170
Cdd:cd00768 75 P-LRLAEIGPAFRNEGGRRGlrRVREFTQLEGEVFGEDgeEASEFEELIELTEELLRALGIKlDIVFVEKtpgEFSPGGA 153
|
....
gi 1084827069 171 RPGY 174
Cdd:cd00768 154 GPGF 157
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
331-409 |
4.10e-17 |
|
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: 76.04 E-value: 4.10e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084827069 331 IALGKEAEMAGTAIIKILREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVIIKDMKTATQDTINLLD 409
Cdd:cd00859 7 VPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETVALDE 85
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
31-313 |
1.30e-16 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 80.75 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 31 FTSYGYSEIKVPVVEKTELFMRSIGEttDIvEKEMYSFLDRHGDGLTLRPEGTASVVRAYIEHKLYTApiNKLFYYGPMF 110
Cdd:PRK12295 18 FEAAGAVRVDPPILQPAEPFLDLSGE--DI-RRRIFVTSDENGEELCLRPDFTIPVCRRHIATAGGEP--ARYAYLGEVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 111 RYerpQKGRYRQFYQIGAEVMG-EDHPFMDAETIEMLVEFFK---------EIGLQGI-TLYINSLGCAecrPGYKQTLT 179
Cdd:PRK12295 93 RQ---RRDRASEFLQAGIESFGrADPAAADAEVLALALEALAalgpgdlevRLGDVGLfAALVDALGLP---PGWKRRLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 180 R------YLEGVKDRLCENCQRRLSV---------NPLRALDC---------------KSTGCIAA-------TQDAPKI 222
Cdd:PRK12295 167 RhfgrprSLDALLARLAGPRVDPLDEhagvlaalaDEAAARALvedlmsiagispvggRSPAEIARrllekaaLAAAARL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 223 TDSLCTRCKQhFIFVTDSL--------------------------SRRGIIA---IPNPRMV------RGLDYYTKTTFE 267
Cdd:PRK12295 247 PAEALAVLER-FLAISGPPdaalaalralaadagldldaaldrfeARLAALAargIDLERLRfsasfgRPLDYYTGFVFE 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1084827069 268 ITAAAGLGAqnAVAAGGRYDGLVKDLGGPA-TPCFGFAMGMERVALL 313
Cdd:PRK12295 326 IRAAGNGDP--PLAGGGRYDGLLTRLGAGEpIPAVGFSIWLDRLAAL 370
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
66-158 |
1.90e-12 |
|
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely threonyl-tRNA members.
Pssm-ID: 395469 [Multi-domain] Cd Length: 181 Bit Score: 65.51 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 66 YSFLDRHGDGLTLRPEGTASVVRAYIEHKL--YTAPInKLFYYGPMFRYERP--QKG--RYRQFYQIGAEVMG--EDHPF 137
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLrsKDLPL-KLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHapGQSPD 79
|
90 100
....*....|....*....|.
gi 1084827069 138 MDAETIEMLVEFFKEIGLQGI 158
Cdd:pfam00587 80 ELEDYIKLIDRVYSRLGLEVR 100
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
23-156 |
5.56e-11 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 62.71 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 23 IEQTACRIFTSYGYSEIKVPVVEKTELfmRSIGEttdivEKEMYSFLDRHGDGLTLRPEGTASVVRAYIEHKLYTAPINK 102
Cdd:PRK12293 25 IENVASEILYENGFEEIVTPFFSYHQH--QSIAD-----EKELIRFSDEKNHQISLRADSTLDVVRIVTKRLGRSTEHKK 97
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1084827069 103 LFYYGPMFRYerPQkgryRQFYQIGAEVMGEDHPfmdAETIEMLVEFFKEIGLQ 156
Cdd:PRK12293 98 WFYIQPVFRY--PS----NEIYQIGAELIGEEDL---SEILNIAAEIFEELELE 142
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
8-360 |
3.61e-08 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 54.98 E-value: 3.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 8 GFNDILPNETFIWKFIEQTACRIFTSYGYSEIKVPVVEKTELFMRSIGETTDIVekeMYSFLDR-HGDGLTLRPEGTASV 86
Cdd:PRK12421 12 GVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQ---TFKLIDQlSGRLMGVRADITPQV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 87 VRayIE-HKLYTAPINKLFYYGPMFRyERPQK-GRYRQFYQIGAEVMGEDHPFMDAETIEMLVEFFKEIGLQGITLYINS 164
Cdd:PRK12421 89 AR--IDaHLLNREGVARLCYAGSVLH-TLPQGlFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGVPALHLDLGH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 165 LGC-----------------------AECRPGYKQ----------------TLTRYLEGVkdrlcENCQRRLSVNPLral 205
Cdd:PRK12421 166 VGIfrrlaelaglspeeeeelfdllqRKALPELAEvcqnlgvgsdlrrmfyALARLNGGL-----EALDRALSVLAL--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 206 dcKSTGCIAATQDAPKITDSLCTRCKQ---HFIfVTDslsrrgiiaipnprmVRGLDYYTKTTFeitAAAGLGAQNAVAA 282
Cdd:PRK12421 238 --QDAAIRQALDELKTLAAHLKNRWPElpvSID-LAE---------------LRGYHYHTGLVF---AAYIPGRGQALAR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 283 GGRYDGLVKDLGG--PATpcfGFAMGMERVALLLQetglrSVKEPplcAFIALGKEAEMAGTAIIKILREDGLRVVEVFT 360
Cdd:PRK12421 297 GGRYDGIGEAFGRarPAT---GFSMDLKELLALQF-----LEEEA---GAILAPWGDDPDLLAAIAELRQQGERVVQLLP 365
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
328-407 |
1.12e-07 |
|
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: 49.51 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 328 CAFIALGKEAEMAGTAIIKI---LREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVIIKDMKTATQDT 404
Cdd:pfam03129 2 VVVIPLGEKAEELEEYAQKLaeeLRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQET 81
|
...
gi 1084827069 405 INL 407
Cdd:pfam03129 82 VSL 84
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
348-407 |
3.65e-07 |
|
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: 47.78 E-value: 3.65e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084827069 348 LREDGLRVVEVFTEGGLKTRMKMADRLGAGFAIILGEDELKTGKVIIKDMKTATQDTINL 407
Cdd:cd00738 27 LLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGESETLHV 86
|
|
| |
