|
Name |
Accession |
Description |
Interval |
E-value |
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
5-411 |
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: 577.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 5 PRGTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDSTDVVQKEMYTFKDKGDRSITLRPEGTAA 84
Cdd:TIGR00442 3 PRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGTAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 85 VVRSYIENKMQGlpNQPVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGLKKLKLVIN 164
Cdd:TIGR00442 83 VARAVIENKLLL--PKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTLEIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 165 SVGDAESRVDYQNALREHFQPVIHNYCKDCQQRIKTNPMRILDCKVDRHQPEIQTAPSITDFLNDYSKDYFEAVKSHLDR 244
Cdd:TIGR00442 161 SLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLDA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 245 LGVPYEVDPKLVRGLDYYTHTAFELMMDNeayDGAITTLCGGGRYNGLLELLDGPSETGIGFALSIERLLLALEEEGIEF 324
Cdd:TIGR00442 241 LGIPYKIDPSLVRGLDYYTGTVFEFVTDD---LGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 325 PQMQHIDLFVATMGEKADDFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATG 404
Cdd:TIGR00442 318 PPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
gi 504426628 405 ESQTMKF 411
Cdd:TIGR00442 398 EQETVPL 404
|
|
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
1-418 |
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: 561.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 1 MIHIPRGTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDstDVVQKEMYTFKDKGDRSITLRPE 80
Cdd:COG0124 3 KIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLRPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 81 GTAAVVRSYIENKmQGLPnQPVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGLKKLK 160
Cdd:COG0124 81 GTAPVARAVAEHG-NELP-FPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDFT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 161 LVINSVGDAESRvdyQNALREHFQ-----PVIHNYCKDCQQRIKTNPMR-ILDCKVDRHQPEIQTAPSITDFLNDYSKDY 234
Cdd:COG0124 159 LEINSRGLPEER---AEALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLAH 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 235 FEAVKSHLDRLGVPYEVDPKLVRGLDYYTHTAFELMMDNEaydGAITTLCGGGRYNGLLELLDGPSETGIGFALSIERLL 314
Cdd:COG0124 236 FEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGL---GAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 315 LALEEEGIEFPQMQHIDLFVATMGEKADDFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAG 394
Cdd:COG0124 313 LLLEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420
....*....|....*....|....
gi 504426628 395 EVAVKHMATGESQTMKFEEIESYI 418
Cdd:COG0124 393 TVTLKDLATGEQETVPLDELVEYL 416
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
6-419 |
5.46e-128 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 376.16 E-value: 5.46e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 6 RGTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDSTDVVQKEMYTFKDKGDRSITLRPEGTAAV 85
Cdd:CHL00201 8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITLRPEGTAGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 86 VRSYIENKMQgLPNQPVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGLKKLKLVINS 165
Cdd:CHL00201 88 VRAFIENKMD-YHSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKNLILDINS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 166 VGDAESRVDYQNALREHFQPVIHNYCKDCQQRIKTNPMRILDCKVDRHQPEIQTAPSITDFLNDYSKDYFEAVKSHLDRL 245
Cdd:CHL00201 167 IGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYDVCTYLNLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 246 GVPYEVDPKLVRGLDYYTHTAFEL-MMDNEAYDgaitTLCGGGRYNGLLELLDGPSETGIGFALSIERLLLALEEEgIEF 324
Cdd:CHL00201 247 NIPYKINYKLVRGLDYYNDTAFEIkTLSSNGQD----TICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAKDN-IIL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 325 PQMQhIDLFVATMGEKADDFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATG 404
Cdd:CHL00201 322 PKQS-IDVYIATQGLKAQKKGWEIIQFLEKQNIKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITIKWLDEQ 400
|
410
....*....|....*
gi 504426628 405 ESQTMKFEEIESYIH 419
Cdd:CHL00201 401 VQENAQYSNFKQEIS 415
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
15-310 |
1.04e-99 |
|
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: 297.98 E-value: 1.04e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 15 ETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDstdVVQKEMYTFKDKGDRSITLRPEGTAAVVRSYIENKM 94
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGD---EVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 95 QGlpNQPVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGLKKLKLVINSVG------- 167
Cdd:cd00773 78 SL--PLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGildgiag 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 168 DAESRVDYQNALRehfqpvihnyckdcqqriktnpmrildckvdrhqpeiqtapsitDFLNDYSKDYFEAVKSHLDRLGV 247
Cdd:cd00773 156 LLEDREEYIERLI--------------------------------------------DKLDKEALAHLEKLLDYLEALGV 191
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504426628 248 --PYEVDPKLVRGLDYYTHTAFELMMDNEaydGAITTLCGGGRYNGLLELLDGPSETGIGFALSI 310
Cdd:cd00773 192 diKYSIDLSLVRGLDYYTGIVFEAVADGL---GAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGL 253
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
5-415 |
6.62e-48 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 170.69 E-value: 6.62e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 5 PRGTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDStdvVQKEMYTFKDKGDRSITLRPEGTAA 84
Cdd:PLN02530 73 PKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEE---ITDQLYNFEDKGGRRVALRPELTPS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 85 VVRSYIEnKMQGLPnQPVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGLKKlklviN 164
Cdd:PLN02530 150 LARLVLQ-KGKSLS-LPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGITS-----S 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 165 SVG-DAESRVDYQNALREHFQPViHNYCKDCQqriktnpmrILDcKVDRHQPE-IQ-----------TAPSITDFLNDYS 231
Cdd:PLN02530 223 DVGiKVSSRKVLQAVLKSYGIPE-ESFAPVCV---------IVD-KLEKLPREeIEkeldtlgvseeAIEGILDVLSLKS 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 232 KDYFEAV-------KSHLDRL-----GVPYE----VDPKLVRGLDYYTHTAFElmmdneAYD--GAITTLCGGGRYNGLL 293
Cdd:PLN02530 292 LDDLEALlgadseaVADLKQLfslaeAYGYQdwlvFDASVVRGLAYYTGIVFE------GFDraGKLRAICGGGRYDRLL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 294 ELLDGPSETGIGFALSIERLLLALEEEGIeFPQMQH-IDLFVATMGEKADDFAVTLLNRLRHAGISVDKDYLSRKLKGQM 372
Cdd:PLN02530 366 STFGGEDTPACGFGFGDAVIVELLKEKGL-LPELPHqVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLEPKKLKWVF 444
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 504426628 373 KQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEEIE 415
Cdd:PLN02530 445 KHAERIGAKRLVLVGASEWERGMVRVKDLSSGEQTEVKLDELE 487
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
9-310 |
1.44e-47 |
|
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA synthetase, found in Bacillus subtilis, Synechocystis sp., Aquifex aeolicus, and others, are in fact a regulatory subunit of ATP phosphoribosyltransferase, and usually encoded by a gene adjacent to that encoding the catalytic subunit. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273081 [Multi-domain] Cd Length: 313 Bit Score: 165.09 E-value: 1.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 9 QDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDStdvvQKEMYTFKDKGDRSITLRPEGTAAVVRS 88
Cdd:TIGR00443 1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGIL----NEDLFKLFDQLGRVLGLRPDMTAPIARL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 89 YIEnKMQGLPnQPVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGLKKLKLVINSVGD 168
Cdd:TIGR00443 77 VST-RLRDRP-LPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELGHVGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 169 AESRVDyQNALREHFQPVIHNYC--KD---CQQRIKTNPMRILDCKVDRHQPEIQ-TAPSITDFLNDYSK--------DY 234
Cdd:TIGR00443 155 VRALLE-EAGLPEEAREALREALarKDlvaLEELVAELGLSPEVRERLLALPRLRgDGEEVLEEARALAGsetaeaalDE 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504426628 235 FEAVKSHLDRLGVPYEV--DPKLVRGLDYYTHTAFELMMDNEAYdgaitTLCGGGRYNGLLELLdGPSETGIGFALSI 310
Cdd:TIGR00443 234 LEAVLELLEARGVEEYIslDLGLVRGYHYYTGLIFEGYAPGLGA-----PLAGGGRYDELLGRF-GRPLPATGFALNL 305
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
7-310 |
2.45e-43 |
|
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: 153.89 E-value: 2.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 7 GTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDSTDvvqkEMYTFKDKGDRSITLRPEGTAAVV 86
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 87 RsyienKMQGLPNQ--PVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGLKKLKLVIN 164
Cdd:pfam13393 77 R-----IDAHRLNRpgPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 165 SVG-------DAESRVDYQNALREHFQPVIHNYCKDC--QQRIKTNPMRILDC---------KVDRHQPEIQTAPSITDf 226
Cdd:pfam13393 152 HVGlvralleAAGLSEALEEALRAALQRKDAAELAELaaEAGLPPALRRALLAlpdlyggpeVLDEARAALPGLPALQE- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 227 lndySKDYFEAVKSHLDRLG--VPYEVDPKLVRGLDYYTHTAFelmmdnEAY-DGAITTLCGGGRYNGLLELLdGPSETG 303
Cdd:pfam13393 231 ----ALDELEALAALLEALGdgVRLTFDLAELRGYEYYTGIVF------AAYaPGVGEPLARGGRYDDLGAAF-GRARPA 299
|
....*..
gi 504426628 304 IGFALSI 310
Cdd:pfam13393 300 TGFSLDL 306
|
|
| 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 ... |
15-310 |
2.85e-41 |
|
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: 146.00 E-value: 2.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 15 ETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARgvGDSTDVVQKEMYTFKDKG----DRSITLRPEGTAAVVRSYI 90
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFK--GGHLDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 91 ENKMQGlPNQPVKLYYNGPMFRYERKQ---KGRYRQFNQFGVEAIGA--ENPSMDAEVLAMVMHIYQSFGLkKLKLVINS 165
Cdd:cd00670 79 GEILSY-RALPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGEpeEAEEERREWLELAEEIARELGL-PVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 166 VGDAESRVDyqnalrehfqpvihnyckdcqqriktnpmrildckvdrhqpeiqtapsitdflndyskdyfeavkshldrl 245
Cdd:cd00670 157 DPFFGRGGK----------------------------------------------------------------------- 165
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504426628 246 gvpyevdpklvRGLDYYTHTAFELMMDNEAYDGAiTTLCGGGRYNGLLEL---------LDGPSETGIGFALSI 310
Cdd:cd00670 166 -----------RGLDAGRETVVEFELLLPLPGRA-KETAVGSANVHLDHFgasfkidedGGGRAHTGCGGAGGE 227
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
1-366 |
6.93e-41 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 149.25 E-value: 6.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 1 MIHIPRGTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFarGVGDSTDVVQKemyTFK---DKGDRSITL 77
Cdd:PRK12292 2 MWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTL--LAGGGAILDLR---TFKlvdQLSGRTLGL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 78 RPEGTAAVVRSyIENKMQGLPNqPVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGLK 157
Cdd:PRK12292 77 RPDMTAQIARI-AATRLANRPG-PLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 158 KLKLVINSVG--------------------DAESRVDYqNALREHFQPVihnyCKDCQQRIKT-----NPMRILDcKVDR 212
Cdd:PRK12292 155 NFTLDLGHVGlfralleaaglseeleevlrRALANKDY-VALEELVLDL----SEELRDALLAlprlrGGREVLE-EARK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 213 --HQPEIQTApsitdfLNDyskdyFEAVKSHLDRLGVPYEV--DPKLVRGLDYYTHTAFelmmdnEAY-DGAITTLCGGG 287
Cdd:PRK12292 229 llPSLPIKRA------LDE-----LEALAEALEKYGYGIPLslDLGLLRHLDYYTGIVF------EGYvDGVGNPIASGG 291
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504426628 288 RYNGLLELLdGPSETGIGFALSIERLLLALeeegIEFPQMQHIDLFVATmGEKADDFAVTLLNRLRHAGISVDKDYLSR 366
Cdd:PRK12292 292 RYDDLLGRF-GRARPATGFSLDLDRLLELQ----LELPVEARKDLVIAP-DSEALAAALAAAQELRKKGEIVVLALPGR 364
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
12-310 |
8.62e-40 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 144.55 E-value: 8.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 12 LPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDSTDvvqKEMYTFKDKGDRSITLRPEGTAAVVRSYIe 91
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVARIAA- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 92 NKMQGLPnQPVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGLKKLKLVINSVG---- 167
Cdd:COG3705 77 TRLANRP-GPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGlfra 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 168 ---DAESRVDYQNALREHFQ----------PVIHNYCKDCQQRIK-----TNPMRILDcKVDR--HQPEIQTApsitdfl 227
Cdd:COG3705 156 lleALGLSEEQREELRRALArkdaveleelLAELGLSEELAEALLalpelYGGEEVLA-RARAllLDAAIRAA------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 228 ndysKDYFEAVKSHLDRLGVPYEV--DPKLVRGLDYYTHTAFelmmdnEAY-DGAITTLCGGGRYNGLLELLdGPSETGI 304
Cdd:COG3705 228 ----LDELEALAEALAARGPDVRLtfDLSELRGYDYYTGIVF------EAYaPGVGDPLARGGRYDGLLAAF-GRARPAT 296
|
....*.
gi 504426628 305 GFALSI 310
Cdd:COG3705 297 GFSLDL 302
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
6-415 |
2.07e-39 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 146.03 E-value: 2.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 6 RGTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDSTDVVqKEMYTFKDKGDRSITLRPEGTAAV 85
Cdd:PRK12420 8 KGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGGGDEIL-KEIYTLTDQGKRDLALRYDLTIPF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 86 VRSYIENkmqglPN--QPVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENPSMDAEVLAMVMHIYQSFGL------- 156
Cdd:PRK12420 87 AKVVAMN-----PNirLPFKRYEIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLevtiqyn 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 157 --KKLKLVINSVG-DAESRVDYQNALREHFQPVIHNYCKDCQQRIKTNPMrildckVDRhqpeiqtapsITDFLN----- 228
Cdd:PRK12420 162 nrKLLNGILQAIGiPTELTSDVILSLDKIEKIGIDGVRKDLLERGISEEM------ADT----------ICNTVLsclql 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 229 --DYSKDYF------------EAVKSHLDRLGVPYEV--DPKLVRGLDYYTHTAFELMMDneayDGAITT-LCGGGRYNG 291
Cdd:PRK12420 226 siADFKEAFnnplvaegvnelQQLQQYLIALGINENCifNPFLARGLTMYTGTVYEIFLK----DGSITSsIGSGGRYDN 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 292 LLELLDGPSE----TGIGFALSIERLLLALEEEGIEFPqmqhiDLFVATMGEKADdfAVTLLNRLRHA-GISVDKDYLSR 366
Cdd:PRK12420 302 IIGAFRGDDMnyptVGISFGLDVIYTALSQKETISSTA-----DVFIIPLGTELQ--CLQIAQQLRSTtGLKVELELAGR 374
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 504426628 367 KLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEEIE 415
Cdd:PRK12420 375 KLKKALNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVPLSSLS 423
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
330-418 |
2.76e-30 |
|
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: 112.25 E-value: 2.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 330 IDLFVATMGEKADDFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTM 409
Cdd:cd00859 2 VDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQETV 81
|
....*....
gi 504426628 410 KFEEIESYI 418
Cdd:cd00859 82 ALDELVEEL 90
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
330-418 |
9.90e-23 |
|
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: 91.69 E-value: 9.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 330 IDLFVATMGEK---ADDFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATGES 406
Cdd:cd00738 2 IDVAIVPLTDPrveAREYAQKLLNALLANGIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTGES 81
|
90
....*....|..
gi 504426628 407 QTMKFEEIESYI 418
Cdd:cd00738 82 ETLHVDELPEFL 93
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
331-418 |
3.97e-18 |
|
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: 78.78 E-value: 3.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 331 DLFVATMGEKAD---DFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATGESQ 407
Cdd:pfam03129 1 QVVVIPLGEKAEeleEYAQKLAEELRAAGIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQE 80
|
90
....*....|.
gi 504426628 408 TMKFEEIESYI 418
Cdd:pfam03129 81 TVSLDELVEKL 91
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
4-404 |
3.71e-15 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 77.62 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 4 IPRGTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFARGVGDSTdvvqKEMYTFKDKGDRSITLRPEGTA 83
Cdd:PLN02972 329 IPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDS----KLIYDLADQGGELCSLRYDLTV 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 84 AVVRsYIenKMQGLPNqpVKLYYNGPMFRYERKQKGRYRQFNQFGVEAIGAENP-SMDAEVLAMVMHIYQSFGLKKLKLV 162
Cdd:PLN02972 405 PFAR-YV--AMNGITS--FKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPmGPDFEIIKVLTELLDELDIGTYEVK 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 163 INSVGDAESRVDYQNALREHFQPVihnyCKDCQQRIKTNPMRILDCKVDRHQPEIQTAPSITDFL--------------- 227
Cdd:PLN02972 480 LNHRKLLDGMLEICGVPPEKFRTI----CSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVkergpplellsklrq 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 228 -------NDYSK---DYFEAVKSHLDRLGVPYEV--DPKLVRGLDYYTHTAFELMmdneaYDGA-ITTLCGGGRYNGLLE 294
Cdd:PLN02972 556 egseflgNASSRaalDELEIMFKALEKSKAIGKIvfDLSLARGLDYYTGVIYEAV-----FKGAqVGSIAAGGRYDNLVG 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 295 LLDGPSETGIGFALSIERLLLALEEEGIEFPQM---QHIDLFVATMGEKADDFAVTLLNRLRHAGISVDKDyLSRKLKGQ 371
Cdd:PLN02972 631 MFSGKQVPAVGVSLGIERVFAIMEQQEEEKSQVirpTETEVLVSIIGDDKLALAAELVSELWNAGIKAEYK-VSTRKAKH 709
|
410 420 430
....*....|....*....|....*....|...
gi 504426628 372 MKQADRLNATYTIVIGDQELEAGEVAVKHMATG 404
Cdd:PLN02972 710 LKRAKESGIPWMVLVGEKELSKGFVKLKNLEAG 742
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
34-308 |
3.94e-15 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 76.51 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 34 NYQEIRTPIFESTDLFARGVGDStdvVQKEMYTFKDKGDRSITLRPEGTAAVVRSYIENKmqglPNQPVKLYYNGPMFRY 113
Cdd:PRK12295 22 GAVRVDPPILQPAEPFLDLSGED---IRRRIFVTSDENGEELCLRPDFTIPVCRRHIATA----GGEPARYAYLGEVFRQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 114 erkQKGRYRQFNQFGVEAIGAENP-SMDAEVLAMVMHIYQSFGLKKLKLVINSVGDAESRVD-------YQNALREHF-Q 184
Cdd:PRK12295 95 ---RRDRASEFLQAGIESFGRADPaAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDalglppgWKRRLLRHFgR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 185 PvihNYCKDCQQRIKTNPMRILDCKVD-----------------------------RHQPEI-------QTAPS------ 222
Cdd:PRK12295 172 P---RSLDALLARLAGPRVDPLDEHAGvlaaladeaaaralvedlmsiagispvggRSPAEIarrllekAALAAaarlpa 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 223 -----ITDFLN-----------------------DYSKDYFEAVKSHLDRLGVPYE---VDPKLVRGLDYYTHTAFELmm 271
Cdd:PRK12295 249 ealavLERFLAisgppdaalaalralaadagldlDAALDRFEARLAALAARGIDLErlrFSASFGRPLDYYTGFVFEI-- 326
|
330 340 350
....*....|....*....|....*....|....*...
gi 504426628 272 dnEAYDGAITTLCGGGRYNGLLELLDGPSET-GIGFAL 308
Cdd:PRK12295 327 --RAAGNGDPPLAGGGRYDGLLTRLGAGEPIpAVGFSI 362
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
19-157 |
2.02e-14 |
|
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA synthetases (aaRS) share a common fold and generally attach an amino acid to the 3' OH of ribose of the appropriate tRNA. PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. These enzymes are usually homodimers. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. The substrate specificity of this reaction is further determined by additional domains. Intererestingly, this domain is also found is asparagine synthase A (AsnA), in the accessory subunit of mitochondrial polymerase gamma and in the bacterial ATP phosphoribosyltransferase regulatory subunit HisZ.
Pssm-ID: 238391 [Multi-domain] Cd Length: 211 Bit Score: 71.77 E-value: 2.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 19 WRYIENQLHKLMEVYNYQEIRTPIFESTDLFARgvgdsTDVVQKEMYTFKDKGDRSITLRPEGTAAVVRSYienkMQGLP 98
Cdd:cd00768 2 RSKIEQKLRRFMAELGFQEVETPIVEREPLLEK-----AGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLF----VSHIR 72
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504426628 99 NQPVKLYYNGPMFRYERKQKG--RYRQFNQFGVEA--IGAENPSMDAEVLAMVMHIYQSFGLK 157
Cdd:cd00768 73 KLPLRLAEIGPAFRNEGGRRGlrRVREFTQLEGEVfgEDGEEASEFEELIELTEELLRALGIK 135
|
|
| tRNA-synt_2b |
pfam00587 |
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ... |
65-162 |
6.46e-13 |
|
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: 66.67 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 65 YTFKDKGDRSITLRPEGTAAVVRSYIEnkmQGL--PNQPVKLYYNGPMFRYERK--QKG--RYRQFNQFGVEAIGAEN-- 136
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFRE---EGLrsKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHAPGqs 77
|
90 100
....*....|....*....|....*.
gi 504426628 137 PSMDAEVLAMVMHIYQSFGLKKLKLV 162
Cdd:pfam00587 78 PDELEDYIKLIDRVYSRLGLEVRVVR 103
|
|
| ThrRS_anticodon |
cd00860 |
ThrRS Threonyl-anticodon binding domain. ThrRS belongs to class II aminoacyl-tRNA synthetases ... |
334-413 |
1.23e-08 |
|
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: 52.12 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 334 VATMGEKADDFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEE 413
Cdd:cd00860 6 VIPVTDEHLDYAKEVAKKLSDAGIRVEVDLRNEKLGKKIREAQLQKIPYILVVGDKEVETGTVSVRTRDGGDLGSMSLDE 85
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
4-157 |
6.29e-08 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 53.85 E-value: 6.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 4 IPRGTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLfaRGVGDStdvvqKEMYTFKDKGDRSITLRPEGTA 83
Cdd:PRK12293 7 IPQGSKLYFGKSAKLKREIENVASEILYENGFEEIVTPFFSYHQH--QSIADE-----KELIRFSDEKNHQISLRADSTL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504426628 84 AVVRsyIENKMQGLPNQPVKLYYNGPMFRYERkqkgryRQFNQFGVEAIGAENPSmdaEVLAMVMHIYQSFGLK 157
Cdd:PRK12293 80 DVVR--IVTKRLGRSTEHKKWFYIQPVFRYPS------NEIYQIGAELIGEEDLS---EILNIAAEIFEELELE 142
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
339-418 |
7.43e-08 |
|
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS 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: 238438 [Multi-domain] Cd Length: 94 Bit Score: 49.90 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 339 EKADDFAVTLLNRLRHAGISV---DKDylsRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEEIE 415
Cdd:cd00861 14 EVQQELAEKLYAELQAAGVDVlldDRN---ERPGVKFADADLIGIPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELL 90
|
...
gi 504426628 416 SYI 418
Cdd:cd00861 91 EFL 93
|
|
| ThrS |
COG0441 |
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA ... |
334-413 |
3.08e-06 |
|
Threonyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Threonyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases
Pssm-ID: 440210 [Multi-domain] Cd Length: 639 Bit Score: 49.26 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 334 VATMGEKADDFAVTLLNRLRHAGISVDKDY----LSRKLKgqmkqadrlNAT-----YTIVIGDQELEAGEVAVKHMATG 404
Cdd:COG0441 544 VLPISDKHADYAKEVAKKLRAAGIRVEVDLrnekIGYKIR---------EAQlqkvpYMLVVGDKEVENGTVSVRRRGGG 614
|
....*....
gi 504426628 405 ESQTMKFEE 413
Cdd:COG0441 615 DLGTMSLDE 623
|
|
| PLN02908 |
PLN02908 |
threonyl-tRNA synthetase |
334-417 |
1.17e-05 |
|
threonyl-tRNA synthetase
Pssm-ID: 178496 [Multi-domain] Cd Length: 686 Bit Score: 47.46 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 334 VATMGEKADDFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEE 413
Cdd:PLN02908 594 VVPISEKSQDYAEEVRAQLHAAGFYVDVDVTDRKIQKKVREAQLAQYNYILVVGEAEAATGTVNVRTRDNVVHGEKKIEE 673
|
....
gi 504426628 414 IESY 417
Cdd:PLN02908 674 LLTE 677
|
|
| ProRS_core |
cd00772 |
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is ... |
6-207 |
2.66e-05 |
|
Prolyl-tRNA synthetase (ProRS) class II core catalytic domain. ProRS is a homodimer. It is responsible for the attachment of proline to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238395 [Multi-domain] Cd Length: 264 Bit Score: 45.44 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 6 RGTQDILPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFaRGVGDSTDVVQKEMYTFKDKGDRSI----TLRPeg 81
Cdd:cd00772 22 RGIINFLPLAKAILDKIENVLDKMFKEHGAQNALFPFFILASFL-EKEAEHDEGFSKELAVFKDAGDEELeedfALRP-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 82 TAAVVRSYIENK-MQGLPNQPVKLYYNGPMFRYE-RKQKG--RYRQFNQFGVEAIGAENPSMDAEVLAMvMHIYQSFgLK 157
Cdd:cd00772 99 TLEENIGEIAAKfIKSWKDLPQHLNQIGNKFRDEiRPRFGflRAREFIMKDGHSAHADAEEADEEFLNM-LSAYAEI-AR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504426628 158 KLKLVINSVGDAESRVDYQNA-----------LREHFQPVIHNYCKDCQQRIKTNPMRILD 207
Cdd:cd00772 177 DLAAIDFIEGEADEGAKFAGAsksrefealmeDGKAKQAETGHIFGEGFARAFDLKAKFLD 237
|
|
| PRK14938 |
PRK14938 |
Ser-tRNA(Thr) hydrolase; Provisional |
343-423 |
4.85e-05 |
|
Ser-tRNA(Thr) hydrolase; Provisional
Pssm-ID: 184902 [Multi-domain] Cd Length: 387 Bit Score: 45.22 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 343 DFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEEIESYIHGGK 422
Cdd:PRK14938 288 DFSIQVAERLRKEGIRVNVDDLDDSLGNKIRRAGTEWIPFVIIIGEREVKTSTLTVKIRANNEQKSMTVEELVKEIKRAD 367
|
.
gi 504426628 423 E 423
Cdd:PRK14938 368 E 368
|
|
| PRK12444 |
PRK12444 |
threonyl-tRNA synthetase; Reviewed |
342-413 |
9.75e-05 |
|
threonyl-tRNA synthetase; Reviewed
Pssm-ID: 183530 [Multi-domain] Cd Length: 639 Bit Score: 44.74 E-value: 9.75e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504426628 342 DDFAVTLLNRLRHAGISVDKDYLSRKLKGQMKQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEE 413
Cdd:PRK12444 555 VQYADEVADKLAQAGIRVERDERDEKLGYKIREAQMQKIPYVLVIGDKEMENGAVNVRKYGEEKSEVIELDM 626
|
|
| PRK03991 |
PRK03991 |
threonyl-tRNA synthetase; Validated |
338-413 |
1.56e-04 |
|
threonyl-tRNA synthetase; Validated
Pssm-ID: 235190 [Multi-domain] Cd Length: 613 Bit Score: 44.09 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 338 GEKADDFAVTLLNRLRHAGISVDKD----YLSRKLKgqmkQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEE 413
Cdd:PRK03991 508 SERHLDYAEEVADKLEAAGIRVDVDdrdeSLGKKIR----DAGKEWIPYVVVIGDKEMESGKLTVTIREESEKVEMTLEE 583
|
|
| Pol_gamma_b_Cterm |
cd02426 |
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for ... |
348-418 |
4.23e-04 |
|
C-terminal domain of mitochondrial DNA polymerase gamma B subunit, which is required for processivity. Polymerase gamma replicates and repairs mitochondrial DNA. The c-terminal domain of its B subunit is strikingly similar to the anticodon-binding domain of glycyl tRNA synthetase.
Pssm-ID: 239106 [Multi-domain] Cd Length: 128 Bit Score: 40.09 E-value: 4.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504426628 348 LLNRLRHAGISVDKDYLSRkLKGQMKQA----DRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEEIESYI 418
Cdd:cd02426 49 LKNELREAGLSVWPGYLET-QHSSLEQLldkyDEMGVLFTLLISEQTLENGLLQLRSRDTTLKETIHISDLPDYL 122
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
339-418 |
1.15e-03 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 41.22 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 339 EKADDFAVTLLNRLRHAGISV---DkdylsRKLK-GQM-KQADRLNATYTIVIGDQELEAGEVAVKHMATGESQTMKFEE 413
Cdd:PRK09194 481 EEVKELAEKLYAELQAAGIEVlldD-----RKERpGVKfADADLIGIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDE 555
|
....*
gi 504426628 414 IESYI 418
Cdd:PRK09194 556 LVEFL 560
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
12-181 |
2.63e-03 |
|
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is responsible for the attachment of threonine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. Class II assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain.
Pssm-ID: 238394 [Multi-domain] Cd Length: 298 Bit Score: 39.46 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 12 LPEETTKWRYIENQLHKLMEVYNYQEIRTPIFESTDLFA-RGvgdSTDVVQKEMYTFkDKGDRSITLRP---EGTAAV-- 85
Cdd:cd00771 26 LPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWEtSG---HWDHYRENMFPF-EEEDEEYGLKPmncPGHCLIfk 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504426628 86 --VRSYIEnkmqgLpnqPVKLYYNGPMFRYErkQKG------RYRQFNQFGVEAIGAENPSMDA--EVLAMVMHIYQSFG 155
Cdd:cd00771 102 skPRSYRD-----L---PLRLAEFGTVHRYE--QSGalhgltRVRGFTQDDAHIFCTPDQIKEEikGVLDLIKEVYSDFG 171
|
170 180 190
....*....|....*....|....*....|.
gi 504426628 156 LKKLKLVI-----NSVGDAESRVDYQNALRE 181
Cdd:cd00771 172 FFDYKVELstrpeKFIGSDEVWEKAEAALRE 202
|
|
| |
