|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-424 |
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: 651.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 2 AKNIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEvtDVVEKEMYTFEDRNGDSLTLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 82 PEGTAGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEHV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL-KDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 162 SLELNSIGSLEARAnyrDALVAFLE-----QHQETLDEDCKRRMYTNPLR-VLDSKNPDVQALLNDAPALGDYLDDDSRE 235
Cdd:COG0124 158 TLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 236 HFAGLCKLLDAAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLL 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 316 VQAVNPEFIASPVVDIYLVAAGAQTQSAAMTLAERLRDEmpGVKLMTNHGGGNFKKQFARADKWGARIALVLGESEVADG 395
Cdd:COG0124 315 LEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420
....*....|....*....|....*....
gi 447029890 396 TVVVKDLRSGEQTAVAQDSVAAHLRTLLG 424
Cdd:COG0124 393 TVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-412 |
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: 633.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 6 QAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGDSLTLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 86 AGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEHVSLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL-KDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 166 NSIGSLEARANYRDALVAFLEQHQETLDEDCKRRMYTNPLRVLDSKNPDVQALLNDAPALGDYLDDDSREHFAGLCKLLD 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 246 AAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQAVNPEFIA 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 326 SPVVDIYLVAAGAQTQSAAMTLAERLRDEmpGVKLMTNHGGGNFKKQFARADKWGARIALVLGESEVADGTVVVKDLRSG 405
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
gi 447029890 406 EQTAVAQ 412
Cdd:TIGR00442 398 EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-407 |
5.41e-145 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 419.69 E-value: 5.41e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 1 MAKnIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGDSLTL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 81 RPEGTAGCVRAGIEHGLLY-NQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGISE 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 160 HVsLELNSIGSLEARANYRDALVAFLEQHQETLDEDCKRRMYTNPLRVLDSKNPDVQALLNDAPALGDYLDDDSREHFAG 239
Cdd:CHL00201 160 LI-LDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 240 LCKLLDAAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQav 319
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAK-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 320 NPEFIASPVVDIYLVAAGAQTQSAAMTLAERLRDEMpgVKLMTNHGGGNFKKQFARADKWGARIALVLGESEVADGTVVV 399
Cdd:CHL00201 317 DNIILPKQSIDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITI 394
|
....*...
gi 447029890 400 KDLRSGEQ 407
Cdd:CHL00201 395 KWLDEQVQ 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-317 |
6.91e-105 |
|
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: 311.07 E-value: 6.91e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 18 ETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRaigEVTDVVEKEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHGL 97
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLR---KSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 98 LYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEHVSLELNSIGSLEARANy 177
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL-KDFQIKINHRGILDGIAG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 178 rdaLVAFLEQHQEtldedckrrmytnplrvldsknpdvqallndapALGDYLDDDSREHFAGLCKLLDAAG--IAYTVNQ 255
Cdd:cd00773 156 ---LLEDREEYIE---------------------------------RLIDKLDKEALAHLEKLLDYLEALGvdIKYSIDL 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447029890 256 RLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ 317
Cdd:cd00773 200 SLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
2.82e-39 |
|
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: 143.11 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDvvekEMYTFEDRNGDSLTLRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 90 RAgIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEHVSLELNSIG 169
Cdd:pfam13393 77 RI-DAHRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV-PGVTLDLGHVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 170 -------SLEARANYRDALVAFLEQHQETLDEDCKRRMYTNP-----LRVLDSKNPDVQALLNDAPAL-GDYLDDDSREH 236
Cdd:pfam13393 155 lvralleAAGLSEALEEALRAALQRKDAAELAELAAEAGLPPalrraLLALPDLYGGPEVLDEARAALpGLPALQEALDE 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447029890 237 FAGLCKLLDAAG--IAYTVNQRLVRGLDYYNRTVFEWVTnsLGSQGTVCAGGRYDGLVEQLgGRATPAVGFAMGLERL 312
Cdd:pfam13393 235 LEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYA--PGVGEPLARGGRYDDLGAAF-GRARPATGFSLDLEAL 309
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HisS |
COG0124 |
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ... |
2-424 |
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: 651.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 2 AKNIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEvtDVVEKEMYTFEDRNGDSLTLR 81
Cdd:COG0124 1 MMKIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGE--DIVEKEMYTFEDRGGRSLTLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 82 PEGTAGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEHV 161
Cdd:COG0124 79 PEGTAPVARAVAEHGNELPFPFKLYYIGPVFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGL-KDF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 162 SLELNSIGSLEARAnyrDALVAFLE-----QHQETLDEDCKRRMYTNPLR-VLDSKNPDVQALLNDAPALGDYLDDDSRE 235
Cdd:COG0124 158 TLEINSRGLPEERA---EALLRYLDkldkiGHEDVLDEDSQRRLETNPLRaILDSKGPDCQEVLADAPKLLDYLGEEGLA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 236 HFAGLCKLLDAAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLL 315
Cdd:COG0124 235 HFEEVLELLDALGIPYVIDPRLVRGLDYYTGTVFEIVTDGLGAQGSVCGGGRYDGLVEQLGGPPTPAVGFAIGLERLLLL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 316 VQAVNPEFIASPVVDIYLVAAGAQTQSAAMTLAERLRDEmpGVKLMTNHGGGNFKKQFARADKWGARIALVLGESEVADG 395
Cdd:COG0124 315 LEELGLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAA--GIRVELDLGGRKLKKQLKYADKSGAPFVLILGEDELANG 392
|
410 420
....*....|....*....|....*....
gi 447029890 396 TVVVKDLRSGEQTAVAQDSVAAHLRTLLG 424
Cdd:COG0124 393 TVTLKDLATGEQETVPLDELVEYLKELLA 421
|
|
| hisS |
TIGR00442 |
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ... |
6-412 |
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: 633.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 6 QAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGDSLTLRPEGT 85
Cdd:TIGR00442 1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 86 AGCVRAGIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEHVSLEL 165
Cdd:TIGR00442 81 APVARAVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGL-KDFTLEI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 166 NSIGSLEARANYRDALVAFLEQHQETLDEDCKRRMYTNPLRVLDSKNPDVQALLNDAPALGDYLDDDSREHFAGLCKLLD 245
Cdd:TIGR00442 160 NSLGILEGRLEYREALIRYLDKHKDKLGEDSVRRLEKNPLRILDSKNEKIQELLKNAPKILDFLCEESRAHFEELKELLD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 246 AAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQAVNPEFIA 325
Cdd:TIGR00442 240 ALGIPYKIDPSLVRGLDYYTGTVFEFVTDDLGAQGSICGGGRYDGLVEELGGPPTPAVGFAIGIERLILLLEELGLIPPP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 326 SPVVDIYLVAAGAQTQSAAMTLAERLRDEmpGVKLMTNHGGGNFKKQFARADKWGARIALVLGESEVADGTVVVKDLRSG 405
Cdd:TIGR00442 320 SKKPDVYVVPLGEEAELEALKLAQKLRKA--GIRVEVDLGGRKLKKQLKYADKLGARFALIIGEDELENGTVTLKDLETG 397
|
....*..
gi 447029890 406 EQTAVAQ 412
Cdd:TIGR00442 398 EQETVPL 404
|
|
| syh |
CHL00201 |
histidine-tRNA synthetase; Provisional |
1-407 |
5.41e-145 |
|
histidine-tRNA synthetase; Provisional
Pssm-ID: 164576 [Multi-domain] Cd Length: 430 Bit Score: 419.69 E-value: 5.41e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 1 MAKnIQAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVEKEMYTFEDRNGDSLTL 80
Cdd:CHL00201 1 MAK-IQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIVNKEMYRFTDRSNRDITL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 81 RPEGTAGCVRAGIEHGLLY-NQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGISE 159
Cdd:CHL00201 80 RPEGTAGIVRAFIENKMDYhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 160 HVsLELNSIGSLEARANYRDALVAFLEQHQETLDEDCKRRMYTNPLRVLDSKNPDVQALLNDAPALGDYLDDDSREHFAG 239
Cdd:CHL00201 160 LI-LDINSIGKLEDRQSYQLKLVEYLSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQEILDGAPKISDFLSLESTEHFYD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 240 LCKLLDAAGIAYTVNQRLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQav 319
Cdd:CHL00201 239 VCTYLNLLNIPYKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTPAVGCAIGLERLLLIAK-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 320 NPEFIASPVVDIYLVAAGAQTQSAAMTLAERLRDEMpgVKLMTNHGGGNFKKQFARADKWGARIALVLGESEVADGTVVV 399
Cdd:CHL00201 317 DNIILPKQSIDVYIATQGLKAQKKGWEIIQFLEKQN--IKFELDLSSSNFHKQIKQAGKKRAKACIILGDNEIMDNCITI 394
|
....*...
gi 447029890 400 KDLRSGEQ 407
Cdd:CHL00201 395 KWLDEQVQ 402
|
|
| HisRS-like_core |
cd00773 |
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ... |
18-317 |
6.91e-105 |
|
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: 311.07 E-value: 6.91e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 18 ETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRaigEVTDVVEKEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHGL 97
Cdd:cd00773 1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLR---KSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 98 LYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEHVSLELNSIGSLEARANy 177
Cdd:cd00773 78 SLPLPLKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGL-KDFQIKINHRGILDGIAG- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 178 rdaLVAFLEQHQEtldedckrrmytnplrvldsknpdvqallndapALGDYLDDDSREHFAGLCKLLDAAG--IAYTVNQ 255
Cdd:cd00773 156 ---LLEDREEYIE---------------------------------RLIDKLDKEALAHLEKLLDYLEALGvdIKYSIDL 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447029890 256 RLVRGLDYYNRTVFEWVTNSLGSQGTVCAGGRYDGLVEQLGGRATPAVGFAMGLERLVLLVQ 317
Cdd:cd00773 200 SLVRGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGGEDVPAVGFAIGLERLLLALE 261
|
|
| 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 ... |
18-317 |
4.45e-48 |
|
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: 164.10 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 18 ETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIgeVTDVVEKEMYTFEDRN----GDSLTLRPEGTAGCVRAGI 93
Cdd:cd00670 1 GTALWRALERFLDDRMAEYGYQEILFPFLAPTVLFFKGG--HLDGYRKEMYTFEDKGrelrDTDLVLRPAACEPIYQIFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 94 EHGLLY-NQEQRLWYIGPMFRHERPQ---KGRYRQFHQLGAEVFGLQG--PDIDAELIMLTARWWRALGisEHVSLELNS 167
Cdd:cd00670 79 GEILSYrALPLRLDQIGPCFRHEPSGrrgLMRVREFRQVEYVVFGEPEeaEEERREWLELAEEIARELG--LPVRVVVAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 168 IGSLEARANyrdalvafleqhqetldedckrrmytnplrvldsknpdvqallndapalgdyldddsrehfaglcklldaa 247
Cdd:cd00670 157 DPFFGRGGK----------------------------------------------------------------------- 165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 248 giaytvnqrlvRGLDYYNRTVFEWVTNSL--GSQGTVCAGGRYDGLVEQ---------LGGRATPAVGFAMGLERLVLLV 316
Cdd:cd00670 166 -----------RGLDAGRETVVEFELLLPlpGRAKETAVGSANVHLDHFgasfkidedGGGRAHTGCGGAGGEERLVLAL 234
|
.
gi 447029890 317 Q 317
Cdd:cd00670 235 L 235
|
|
| hisZ_biosyn_reg |
TIGR00443 |
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ... |
13-317 |
7.05e-45 |
|
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: 158.16 E-value: 7.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 13 DYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEqtplFKRAIGEVTDVVEKEMYTFEDRNGDSLTLRPEGTAGCVRAG 92
Cdd:TIGR00443 2 DLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLE----YLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 93 IEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGISE------HVSL--E 164
Cdd:TIGR00443 78 STRLRDRPLPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDfkielgHVGLvrA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 165 L--NSIGSLEARANYRDAL----VAFLEQHQETLDEDCKRRMYTNPLRVLDSKNPDV----QALLNDAPALGdYLDDDSR 234
Cdd:TIGR00443 158 LleEAGLPEEAREALREALarkdLVALEELVAELGLSPEVRERLLALPRLRGDGEEVleeaRALAGSETAEA-ALDELEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 235 ehfagLCKLLDAAGI--AYTVNQRLVRGLDYYNRTVFEWVTNSLGSqgTVCAGGRYDGLVEQLgGRATPAVGFAMGLERL 312
Cdd:TIGR00443 237 -----VLELLEARGVeeYISLDLGLVRGYHYYTGLIFEGYAPGLGA--PLAGGGRYDELLGRF-GRPLPATGFALNLERL 308
|
....*
gi 447029890 313 VLLVQ 317
Cdd:TIGR00443 309 LEALT 313
|
|
| PLN02530 |
PLN02530 |
histidine-tRNA ligase |
9-414 |
1.56e-43 |
|
histidine-tRNA ligase
Pssm-ID: 178145 [Multi-domain] Cd Length: 487 Bit Score: 158.75 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 9 RGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGE-VTDvvekEMYTFEDRNGDSLTLRPEGTAG 87
Cdd:PLN02530 74 KGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEeITD----QLYNFEDKGGRRVALRPELTPS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 88 CVRAGIEHGllynQEQRL---WY-IGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGI-SEHVS 162
Cdd:PLN02530 150 LARLVLQKG----KSLSLplkWFaIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGItSSDVG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 163 LELNSIGSLEA---RANYRDALVAF------------LEQHQETLDE-DCKRRMYTNPLRVLDSKN-PDVQALLndaPAL 225
Cdd:PLN02530 226 IKVSSRKVLQAvlkSYGIPEESFAPvcvivdkleklpREEIEKELDTlGVSEEAIEGILDVLSLKSlDDLEALL---GAD 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 226 GDYLDDDSRehfagLCKLLDAAGIA--YTVNQRLVRGLDYYNRTVFEWVTNSlGSQGTVCAGGRYDGLVEQLGGRATPAV 303
Cdd:PLN02530 303 SEAVADLKQ-----LFSLAEAYGYQdwLVFDASVVRGLAYYTGIVFEGFDRA-GKLRAICGGGRYDRLLSTFGGEDTPAC 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 304 GFAMGLERLVLLVQ--AVNPEFiaSPVVDIYLVAAGAQTQSAAMTLAERLRDEMPGVKLMTNhgGGNFKKQFARADKWGA 381
Cdd:PLN02530 377 GFGFGDAVIVELLKekGLLPEL--PHQVDDVVFALDEDLQGAAAGVASRLREKGRSVDLVLE--PKKLKWVFKHAERIGA 452
|
410 420 430
....*....|....*....|....*....|...
gi 447029890 382 RIALVLGESEVADGTVVVKDLRSGEQTAVAQDS 414
Cdd:PLN02530 453 KRLVLVGASEWERGMVRVKDLSSGEQTEVKLDE 485
|
|
| hisZ |
PRK12292 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
10-354 |
2.06e-40 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237043 [Multi-domain] Cd Length: 391 Bit Score: 148.09 E-value: 2.06e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGevtDVVEKEMYTFEDR-NGDSLTLRPEGTAGC 88
Cdd:PRK12292 8 GIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGG---AILDLRTFKLVDQlSGRTLGLRPDMTAQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 89 VRAgIEHGLLYNQE-QRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGISE------HV 161
Cdd:PRK12292 85 ARI-AATRLANRPGpLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNftldlgHV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 162 SLeLNSI-----GSLEARANYRDALVAF----LEQHQETLDEDCKR------RMYtNPLRVLDsknpDVQALLNDAPALG 226
Cdd:PRK12292 164 GL-FRALleaagLSEELEEVLRRALANKdyvaLEELVLDLSEELRDallalpRLR-GGREVLE----EARKLLPSLPIKR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 227 DyLDDdsrehFAGLCKLLDAAGIAYTVNQRL--VRGLDYYNRTVFEWVTNSLGSQgtVCAGGRYDGLVEQLgGRATPAVG 304
Cdd:PRK12292 238 A-LDE-----LEALAEALEKYGYGIPLSLDLglLRHLDYYTGIVFEGYVDGVGNP--IASGGRYDDLLGRF-GRARPATG 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 447029890 305 FAMGLERLVLLVQAVNPefiasPVVDIYLVAAGAQTQSAAMTLAERLRDE 354
Cdd:PRK12292 309 FSLDLDRLLELQLELPV-----EARKDLVIAPDSEALAAALAAAQELRKK 353
|
|
| tRNA-synt_His |
pfam13393 |
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ... |
10-312 |
2.82e-39 |
|
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: 143.11 E-value: 2.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDvvekEMYTFEDRNGDSLTLRPEGTAGCV 89
Cdd:pfam13393 1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLD----QTFKLVDQSGRLLGLRADITPQVA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 90 RAgIEHGLLYNQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEHVSLELNSIG 169
Cdd:pfam13393 77 RI-DAHRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGV-PGVTLDLGHVG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 170 -------SLEARANYRDALVAFLEQHQETLDEDCKRRMYTNP-----LRVLDSKNPDVQALLNDAPAL-GDYLDDDSREH 236
Cdd:pfam13393 155 lvralleAAGLSEALEEALRAALQRKDAAELAELAAEAGLPPalrraLLALPDLYGGPEVLDEARAALpGLPALQEALDE 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447029890 237 FAGLCKLLDAAG--IAYTVNQRLVRGLDYYNRTVFEWVTnsLGSQGTVCAGGRYDGLVEQLgGRATPAVGFAMGLERL 312
Cdd:pfam13393 235 LEALAALLEALGdgVRLTFDLAELRGYEYYTGIVFAAYA--PGVGEPLARGGRYDDLGAAF-GRARPATGFSLDLEAL 309
|
|
| HisZ |
COG3705 |
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism]; |
15-318 |
1.41e-38 |
|
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
Pssm-ID: 442919 [Multi-domain] Cd Length: 312 Bit Score: 141.08 E-value: 1.41e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 15 LPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDvveKEMYTFEDRNGDSLTLRPEGTAGCVRAGIE 94
Cdd:COG3705 1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLD---LQTFKLVDQLGRTLGLRPDMTPQVARIAAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 95 HglLYNQE--QRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEHVSLELNSIG--- 169
Cdd:COG3705 78 R--LANRPgpLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGL-EDFTLDLGHVGlfr 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 170 ----SLEARANYRDALVAFLEQ----------HQETLDEDCKRRMY-----TNPLRVLDsknpDVQALLNDAPALgdyld 230
Cdd:COG3705 155 alleALGLSEEQREELRRALARkdaveleellAELGLSEELAEALLalpelYGGEEVLA----RARALLLDAAIR----- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 231 dDSREHFAGLCKLLDAAGIA--YTVNQRLVRGLDYYNRTVFEWVTNSLGsqGTVCAGGRYDGLVEQLGgRATPAVGFAMG 308
Cdd:COG3705 226 -AALDELEALAEALAARGPDvrLTFDLSELRGYDYYTGIVFEAYAPGVG--DPLARGGRYDGLLAAFG-RARPATGFSLD 301
|
330
....*....|
gi 447029890 309 LERLVLLVQA 318
Cdd:COG3705 302 LDRLLRALPA 311
|
|
| PRK12420 |
PRK12420 |
histidyl-tRNA synthetase; Provisional |
6-415 |
1.51e-38 |
|
histidyl-tRNA synthetase; Provisional
Pssm-ID: 237097 [Multi-domain] Cd Length: 423 Bit Score: 143.72 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 6 QAIRGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLF--KRAIGevtDVVEKEMYTFEDRNGDSLTLRPE 83
Cdd:PRK12420 5 RNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMssKYGGG---DEILKEIYTLTDQGKRDLALRYD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 84 GTAGCVRAgiehgLLYNQEQRLWY----IGPMFRHERPQKGRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGISe 159
Cdd:PRK12420 82 LTIPFAKV-----VAMNPNIRLPFkryeIGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLE- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 160 hVSLELNSIGSLearANYRDALVAFLEQHQE---TLD--EDCKRRMYTNPLRVLDSKNPDVQALLNDAPALGDYLDDDSR 234
Cdd:PRK12420 156 -VTIQYNNRKLL---NGILQAIGIPTELTSDvilSLDkiEKIGIDGVRKDLLERGISEEMADTICNTVLSCLQLSIADFK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 235 EHFAG------------LCKLLDAAGIA--YTVNQRLVRGLDYYNRTVFEW------VTNSLGSqgtvcaGGRYDGLVEQ 294
Cdd:PRK12420 232 EAFNNplvaegvnelqqLQQYLIALGINenCIFNPFLARGLTMYTGTVYEIflkdgsITSSIGS------GGRYDNIIGA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 295 LGG--RATPAVGFAMGLErlvLLVQAVNPEFIASPVVDIYLVAAGAQTQSAAMtlAERLRdEMPGVKLMTNHGGGNFKKQ 372
Cdd:PRK12420 306 FRGddMNYPTVGISFGLD---VIYTALSQKETISSTADVFIIPLGTELQCLQI--AQQLR-STTGLKVELELAGRKLKKA 379
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 447029890 373 FARADKWGARIALVLGESEVADGTVVVKDLRSGEQTAVAQDSV 415
Cdd:PRK12420 380 LNYANKENIPYVLIIGEEEVSTGTVMLRNMKEGSEVKVPLSSL 422
|
|
| class_II_aaRS-like_core |
cd00768 |
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ... |
21-173 |
5.27e-38 |
|
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: 136.86 E-value: 5.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 21 IWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEvtdvvEKEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHglLYN 100
Cdd:cd00768 1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHE-----PKDLLPVGAENEEDLYLRPTLEPGLVRLFVSH--IRK 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447029890 101 QEQRLWYIGPMFRHERPQKG--RYRQFHQLGAEVFGLQGPD--IDAELIMLTARWWRALGISEHVSLELNSIGSLEA 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 ... |
68-320 |
1.32e-35 |
|
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: 129.45 E-value: 1.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 68 YTFEDRNGDSLTLRPEGTAGCVRAGIEHGL-LYNQEQRLWYIGPMFRHERP--QKG--RYRQFHQLGAEVFGLQG--PDI 140
Cdd:pfam00587 1 YKVEDENGDELALKPTNEPGHTLLFREEGLrSKDLPLKLAQFGTCFRHEASgdTRGliRVRQFHQDDAHIFHAPGqsPDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 141 DAELIMLTARWWRALGISEHVSLELNSIGSlearanyrdalvafleqhqetldedckrrmytnplrvldsknpdvqalln 220
Cdd:pfam00587 81 LEDYIKLIDRVYSRLGLEVRVVRLSNSDGS-------------------------------------------------- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 221 dapalgdyldddsrehfaglcklldaagiaytvnqrlvrgLDYYNRTVFEWVTNSLGSQG-TVCAGGRYDGLVEQLGGRA 299
Cdd:pfam00587 111 ----------------------------------------AFYGPKLDFEVVFPSLGKQRqTGTIQNDGFRLPRRLGIRY 150
|
250 260 270
....*....|....*....|....*....|.
gi 447029890 300 --------TP-AVGFA-MGLERLVLLVQAVN 320
Cdd:pfam00587 151 kdedneskFPyMIHRAgLGVERFLAAILENN 181
|
|
| HisRS_anticodon |
cd00859 |
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ... |
328-420 |
8.80e-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: 113.40 E-value: 8.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 328 VVDIYLVAAGAQTQSAAMTLAERLRDEmpGVKLMTNHGGGNFKKQFARADKWGARIALVLGESEVADGTVVVKDLRSGEQ 407
Cdd:cd00859 1 EVDVYVVPLGEGALSEALELAEQLRDA--GIKAEIDYGGRKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQ 78
|
90
....*....|...
gi 447029890 408 TAVAQDSVAAHLR 420
Cdd:cd00859 79 ETVALDELVEELK 91
|
|
| PLN02972 |
PLN02972 |
Histidyl-tRNA synthetase |
9-423 |
1.48e-24 |
|
Histidyl-tRNA synthetase
Pssm-ID: 215525 [Multi-domain] Cd Length: 763 Bit Score: 106.51 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 9 RGMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTdvveKEMYTFEDRNGDSLTLRPEGTAGC 88
Cdd:PLN02972 331 KGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDS----KLIYDLADQGGELCSLRYDLTVPF 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 89 VRAGIEHGLlynQEQRLWYIGPMFRHERPQKGRYRQFHQLGAEVFGLQGP-DIDAELIMLtarwwralgISEHVSlELNs 167
Cdd:PLN02972 407 ARYVAMNGI---TSFKRYQIAKVYRRDNPSKGRYREFYQCDFDIAGVYEPmGPDFEIIKV---------LTELLD-ELD- 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 168 IGSLEARANYRDALVAFLE-------------QHQETLD----EDCKRRMYTN---PLRVLD-------SKNPDVQALLN 220
Cdd:PLN02972 473 IGTYEVKLNHRKLLDGMLEicgvppekfrticSSIDKLDkqsfEQVKKEMVEEkglSNETADkignfvkERGPPLELLSK 552
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 221 ----DAPALGDYLDDDSREHFAGLCKLLDAAGI--AYTVNQRLVRGLDYYNRTVFEWVTNslGSQ-GTVCAGGRYDGLVE 293
Cdd:PLN02972 553 lrqeGSEFLGNASSRAALDELEIMFKALEKSKAigKIVFDLSLARGLDYYTGVIYEAVFK--GAQvGSIAAGGRYDNLVG 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 294 QLGGRATPAVGFAMGLERLVLLVQAVNPEfiASPVV-----DIYLVAAGAQTQSAAMTLAERL-----RDEMPGVKLMTN 363
Cdd:PLN02972 631 MFSGKQVPAVGVSLGIERVFAIMEQQEEE--KSQVIrptetEVLVSIIGDDKLALAAELVSELwnagiKAEYKVSTRKAK 708
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 364 HgggnfkkqFARADKWGARIALVLGESEVADGTVVVKDLRSGEQTAVAQDSVAAHLRTLL 423
Cdd:PLN02972 709 H--------LKRAKESGIPWMVLVGEKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAEL 760
|
|
| hisZ |
PRK12295 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
65-318 |
1.00e-15 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183413 [Multi-domain] Cd Length: 373 Bit Score: 78.05 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 65 KEMYTFEDRNGDSLTLRPEGTAGCVRAGIEHGLlyNQEQRLWYIGPMFRHerpQKGRYRQFHQLGAEVFGLQGP-DIDAE 143
Cdd:PRK12295 47 RRIFVTSDENGEELCLRPDFTIPVCRRHIATAG--GEPARYAYLGEVFRQ---RRDRASEFLQAGIESFGRADPaAADAE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 144 LIMLTARWWRALGISEhVSLELNSIGSLEA--------------------RANYRDALVAFL--------EQHQETL--- 192
Cdd:PRK12295 122 VLALALEALAALGPGD-LEVRLGDVGLFAAlvdalglppgwkrrllrhfgRPRSLDALLARLagprvdplDEHAGVLaal 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 193 -DEDCKRRMYTNPL------------------RVL--------DSKNPDVQALLNDAPALGDYLDDDSR--EHFAGLCKL 243
Cdd:PRK12295 201 aDEAAARALVEDLMsiagispvggrspaeiarRLLekaalaaaARLPAEALAVLERFLAISGPPDAALAalRALAADAGL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 244 ---------------LDAAGI---AYTVNQRLVRGLDYYNRTVFEWVTNSLGSqGTVCAGGRYDGLVEQLG-GRATPAVG 304
Cdd:PRK12295 281 dldaaldrfearlaaLAARGIdleRLRFSASFGRPLDYYTGFVFEIRAAGNGD-PPLAGGGRYDGLLTRLGaGEPIPAVG 359
|
330
....*....|....
gi 447029890 305 FAMGLERLVLLVQA 318
Cdd:PRK12295 360 FSIWLDRLAALGGA 373
|
|
| HGTP_anticodon |
pfam03129 |
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ... |
328-422 |
6.15e-11 |
|
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: 58.75 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 328 VVDIYLVAAGAQTQSAAMTLAERLRDEmpGVKLMTNHGGGNFKKQFARADKWGARIALVLGESEVADGTVVVKDLRSGEQ 407
Cdd:pfam03129 2 VVVIPLGEKAEELEEYAQKLAEELRAA--GIRVELDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79
|
90
....*....|....*
gi 447029890 408 TAVAQDSVAAHLRTL 422
Cdd:pfam03129 80 ETVSLDELVEKLKEL 94
|
|
| PRK12421 |
PRK12421 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
10-354 |
2.08e-10 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 237098 Cd Length: 392 Bit Score: 61.91 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKRAIGEVTDVVekemyTFedRNGDSLTLRPEGtagcV 89
Cdd:PRK12421 12 GVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQ-----TF--KLIDQLSGRLMG----V 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 90 RAGI--------EHGLLYNQEQRLWYIGPMFrHERPQK-GRYRQFHQLGAEVFGLQGPDIDAELIMLTARWWRALGIsEH 160
Cdd:PRK12421 81 RADItpqvaridAHLLNREGVARLCYAGSVL-HTLPQGlFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGV-PA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 161 VSLELNSIG---SLEARA----NYRDALVAFLEQH-QETLDEDCKRRMYTNPLR----VLDSKNPDVQALLNDAPALGDY 228
Cdd:PRK12421 159 LHLDLGHVGifrRLAELAglspEEEEELFDLLQRKaLPELAEVCQNLGVGSDLRrmfyALARLNGGLEALDRALSVLALQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 229 lDDDSREHFAGLCKLLDAAGIAYT---VNQRLV--RGLDYYNRTVFEWVTNSLGSQgtVCAGGRYDGlVEQLGGRATPAV 303
Cdd:PRK12421 239 -DAAIRQALDELKTLAAHLKNRWPelpVSIDLAelRGYHYHTGLVFAAYIPGRGQA--LARGGRYDG-IGEAFGRARPAT 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 447029890 304 GFAMGLERLVLLVQAVnpefiaSPVVDIYLVAAGAQTQSAAMtlaERLRDE 354
Cdd:PRK12421 315 GFSMDLKELLALQFLE------EEAGAILAPWGDDPDLLAAI---AELRQQ 356
|
|
| HGTP_anticodon |
cd00738 |
HGTP anticodon binding domain, as found at the C-terminus of histidyl, glycyl, threonyl and ... |
329-420 |
3.59e-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: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 329 VDIYLVAAGAQTQSA---AMTLAERLRDEmpGVKLMTNHGGGNFKKQFARADKWGARIALVLGESEVADGTVVVKDLRSG 405
Cdd:cd00738 2 IDVAIVPLTDPRVEAreyAQKLLNALLAN--GIRVLYDDRERKIGKKFREADLRGVPFAVVVGEDELENGKVTVKSRDTG 79
|
90
....*....|....*
gi 447029890 406 EQTAVAQDSVAAHLR 420
Cdd:cd00738 80 ESETLHVDELPEFLV 94
|
|
| hisZ |
PRK12293 |
ATP phosphoribosyltransferase regulatory subunit; Provisional |
17-307 |
9.48e-06 |
|
ATP phosphoribosyltransferase regulatory subunit; Provisional
Pssm-ID: 183411 Cd Length: 281 Bit Score: 46.91 E-value: 9.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 17 GETA-IWQRIEGTLKNVLGSYGYSEIrlpiveQTPLFKRAIGE-VTDvvEKEMYTFEDRNGDSLTLRPEGTAGCVRAgIE 94
Cdd:PRK12293 16 GKSAkLKREIENVASEILYENGFEEI------VTPFFSYHQHQsIAD--EKELIRFSDEKNHQISLRADSTLDVVRI-VT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 95 HGLLYNQEQRLW-YIGPMFRHerPQkgryRQFHQLGAEVFGlqGPDIdAELIMLTARWWRALGISEHVSLELNSIGSLEA 173
Cdd:PRK12293 87 KRLGRSTEHKKWfYIQPVFRY--PS----NEIYQIGAELIG--EEDL-SEILNIAAEIFEELELEPILQISNIKIPKLVA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 174 RaNYRDALVAFLEQHQETLDEdcKRRMYTNPLRVLdsKNP-DVQALLNDAPalgdyldDDSREHfagLCKLLD-AAGIAY 251
Cdd:PRK12293 158 E-ILGLDIEVFKKGQIEKLLA--QNVPWLNKLVRI--KTLeDLDEVIELVP-------DEIKEE---LEKLKElAESIKY 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 447029890 252 TvNQRLV----RGLDYYNRTVFEWVTNSLgsqgTVCAGGRY--DGLveqlggratPAVGFAM 307
Cdd:PRK12293 223 E-NLVIAplyyAKMRYYDDLFFRFFDGNS----TLASGGNYeiDGI---------SSSGFAL 270
|
|
| PRK09194 |
PRK09194 |
prolyl-tRNA synthetase; Provisional |
330-424 |
2.37e-05 |
|
prolyl-tRNA synthetase; Provisional
Pssm-ID: 236405 [Multi-domain] Cd Length: 565 Bit Score: 46.62 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 330 DIYLVAAGAQTQsAAMTLAERL---------------RDEMPGVKlmtnhgggnfkkqFARADKWGARIALVLGESEVAD 394
Cdd:PRK09194 470 DVHIVPVNMKDE-EVKELAEKLyaelqaagievllddRKERPGVK-------------FADADLIGIPHRIVVGDRGLAE 535
|
90 100 110
....*....|....*....|....*....|
gi 447029890 395 GTVVVKDLRSGEQTAVAQDSVAAHLRTLLG 424
Cdd:PRK09194 536 GIVEYKDRRTGEKEEVPVDELVEFLKALKK 565
|
|
| ProRS_anticodon_short |
cd00861 |
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ... |
328-415 |
7.76e-04 |
|
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: 38.34 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 328 VVDIYLVAAGAQTQSAAMTLAERL-----------RDEMPGVKlmtnhgggnfkkqFARADKWGARIALVLGESEVADGT 396
Cdd:cd00861 4 VVIIPMNMKDEVQQELAEKLYAELqaagvdvllddRNERPGVK-------------FADADLIGIPYRIVVGKKSAAEGI 70
|
90
....*....|....*....
gi 447029890 397 VVVKDLRSGEQTAVAQDSV 415
Cdd:cd00861 71 VEIKVRKTGEKEEISIDEL 89
|
|
| ThrRS_core |
cd00771 |
Threonyl-tRNA synthetase (ThrRS) class II core catalytic domain. ThrRS is a homodimer. It is ... |
10-133 |
3.07e-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: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029890 10 GMNDYLPGETAIWQRIEGTLKNVLGSYGYSEIRLPIVEQTPLFKraIGEVTDVVEKEMYTFEdRNGDSLTLRPegtAGCV 89
Cdd:cd00771 21 GLPFWLPKGAIIRNELEDFLRELQRKRGYQEVETPIIYNKELWE--TSGHWDHYRENMFPFE-EEDEEYGLKP---MNCP 94
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 447029890 90 ragiEHGLLYNQEQRLWY--------IGPMFRHErpQKG------RYRQFHQLGAEVF 133
Cdd:cd00771 95 ----GHCLIFKSKPRSYRdlplrlaeFGTVHRYE--QSGalhgltRVRGFTQDDAHIF 146
|
|
| |
