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Conserved domains on  [gi|1391723582|ref|NP_001350465|]
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histidine--tRNA ligase, mitochondrial isoform 5 [Homo sapiens]

Protein Classification

histidine--tRNA ligase( domain architecture ID 1007767)

histidine--tRNA ligase (HisRS) is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA

CATH:  3.40.50.800|3.30.930.10
EC:  6.1.1.21
Gene Ontology:  GO:0003723|GO:0042802|GO:0004821|GO:0006427|GO:0005524|GO:0006412

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02972 super family cl33611
Histidyl-tRNA synthetase
 1-434 6.74e-178

Histidyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02972:

Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 515.98  E-value: 6.74e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKR 80
Cdd:PLN02972  341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  81 YHVGKVWRRESPTivQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPES 160
Cdd:PLN02972  421 YQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 161 KFRAICSSIDKLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972  499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 239 YLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVE 318
Cdd:PLN02972  579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIE 647

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 319 RIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIG 398
Cdd:PLN02972  648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1391723582 399 EQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLS 434
Cdd:PLN02972  726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELL 761
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 1-434 6.74e-178

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 515.98  E-value: 6.74e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKR 80
Cdd:PLN02972  341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  81 YHVGKVWRRESPTivQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPES 160
Cdd:PLN02972  421 YQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 161 KFRAICSSIDKLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972  499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 239 YLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVE 318
Cdd:PLN02972  579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIE 647

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 319 RIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIG 398
Cdd:PLN02972  648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1391723582 399 EQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLS 434
Cdd:PLN02972  726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELL 761
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 1-435 2.02e-106

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: 321.30  E-value: 2.02e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTVPFARYLAMNK---V 75
Cdd:COG0124    18 SAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGnelP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  76 KKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLIKVNDRrivdgmfav 154
Cdd:COG0124    98 FPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR--------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 155 cGVPESKFRAICSSIDKLDKMAWKDVrhemvvkkgLAPEVADRIG-----DYVQCHGGV--SLVEQMfqdPRLSQNKqAL 227
Cdd:COG0124   165 -GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLADA---PKLLDYL-GE 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 228 EGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHK 307
Cdd:COG0124   231 EGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPP 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 308 VPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCE 387
Cdd:COG0124   299 TPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYAD 374

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1391723582 388 STGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSE 435
Cdd:COG0124   375 KSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 1-325 7.56e-97

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: 291.04  E-value: 7.56e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 77
Cdd:cd00773     2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  78 -MKRYHVGKVWRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaVCG 156
Cdd:cd00773    82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 157 VPESKFRAICSSIDKLDKmawkdvrhemvvkkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLGDLKLL 236
Cdd:cd00773   156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 237 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 316
Cdd:cd00773   183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252


                  ....*....
gi 1391723582 317 VERIFYIVE 325
Cdd:cd00773   253 LERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 1-422 3.24e-87

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: 271.27  E-value: 3.24e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLTVPFARYLAMNK-- 74
Cdd:TIGR00442  14 MIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGTAPVARAVIENKll 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  75 -VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMF 152
Cdd:TIGR00442  94 lPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 153 AvcgvpesKFRAICSSIDK-LDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQchggvslveqmfQDPRLSQNKQAlEGLG 231
Cdd:TIGR00442 170 E-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAPKILDFLCE-ESRA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 232 DLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCV 311
Cdd:TIGR00442 230 HFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAV 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 312 GLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCESTGI 391
Cdd:TIGR00442 298 GFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGA 373

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1391723582 392 PLVVIIGEQELKEGVIKIRSVASREEVAIKR 422
Cdd:TIGR00442 374 RFALIIGEDELENGTVTLKDLETGEQETVPL 404
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 3-320 1.29e-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: 138.87  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   3 VREKILDLviscFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA--MNKVKKMKR 80
Cdd:pfam13393  16 LRRRLLDL----FRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDAhrLNRPGPLRL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  81 YHVGKVWRRESPTIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPES 160
Cdd:pfam13393  92 CYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 161 KFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEGLGDLKLLFEYL 240
Cdd:pfam13393 169 LEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAALL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 241 TLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVPCVGLSIGVERI 320
Cdd:pfam13393 243 EALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 1-434 6.74e-178

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 515.98  E-value: 6.74e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKR 80
Cdd:PLN02972  341 MAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVAMNGITSFKR 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  81 YHVGKVWRRESPTivQGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPES 160
Cdd:PLN02972  421 YQIAKVYRRDNPS--KGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGMLEICGVPPE 498

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 161 KFRAICSSIDKLDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQCHGG-VSLVEQMFQ-DPRLSQNKQALEGLGDLKLLFE 238
Cdd:PLN02972  499 KFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNASSRAALDELEIMFK 578

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 239 YLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTptqageeplNVGSVAAGGRYDGLVGMFDPKghKVPCVGLSIGVE 318
Cdd:PLN02972  579 ALEKSKAIGKIVFDLSLARGLDYYTGVIYEAVFKGA---------QVGSIAAGGRYDNLVGMFSGK--QVPAVGVSLGIE 647

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 319 RIFYIVEQRMKTKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEmlYKNNPKLLTQLHYCESTGIPLVVIIG 398
Cdd:PLN02972  648 RVFAIMEQQEEEKSQVIRPTETEVLVSIIGDDKLALAAELVSELWNAGIKAE--YKVSTRKAKHLKRAKESGIPWMVLVG 725

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 1391723582 399 EQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLS 434
Cdd:PLN02972  726 EKELSKGFVKLKNLEAGVEEEVDRTCFVQELKAELL 761
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 1-435 2.02e-106

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: 321.30  E-value: 2.02e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG--LMYDLKDQGGELLSLRYDLTVPFARYLAMNK---V 75
Cdd:COG0124    18 SAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVekEMYTFEDRGGRSLTLRPEGTAPVARAVAEHGnelP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  76 KKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLIKVNDRrivdgmfav 154
Cdd:COG0124    98 FPFKLYYIGPVFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDFTLEINSR--------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 155 cGVPESKFRAICSSIDKLDKMAWKDVrhemvvkkgLAPEVADRIG-----DYVQCHGGV--SLVEQMfqdPRLSQNKqAL 227
Cdd:COG0124   165 -GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLEtnplrAILDSKGPDcqEVLADA---PKLLDYL-GE 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 228 EGLGDLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHK 307
Cdd:COG0124   231 EGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQ--------GSVCGGGRYDGLVEQLG--GPP 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 308 VPCVGLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCE 387
Cdd:COG0124   299 TPAVGFAIGLERLLLLLEEL---GLLPAAEPPPDVYVVPLGEEARAEALKLAQELRAAGIRVELDLGGR-KLKKQLKYAD 374

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1391723582 388 STGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLSE 435
Cdd:COG0124   375 KSGAPFVLILGEDELANGTVTLKDLATGEQETVPLDELVEYLKELLAE 422
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 1-325 7.56e-97

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: 291.04  E-value: 7.56e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSG-LMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKK-- 77
Cdd:cd00773     2 AALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSkEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSLpl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  78 -MKRYHVGKVWRRESPTivQGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGmfaVCG 156
Cdd:cd00773    82 pLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IAG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 157 VPESKFRAICSSIDKLDKmawkdvrhemvvkkglapevadrigdyvqchggvslveqmfqdprlsqnkqalEGLGDLKLL 236
Cdd:cd00773   156 LLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEKL 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 237 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG 316
Cdd:cd00773   183 LDYLEALGVDIKYSIDLSLVRGLDYYTGIVFEAVADGLGAQ--------GSIAGGGRYDGLLEEFG--GEDVPAVGFAIG 252


                  ....*....
gi 1391723582 317 VERIFYIVE 325
Cdd:cd00773   253 LERLLLALE 261
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 1-422 3.24e-87

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: 271.27  E-value: 3.24e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   1 MVVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLTVPFARYLAMNK-- 74
Cdd:TIGR00442  14 MIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEETDIvskeMYTFKDKGGRSLTLRPEGTAPVARAVIENKll 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  75 -VKKMKRYHVGKVWRRESPtivQ-GRYREFCQCDFDIAGQFDPMIpDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMF 152
Cdd:TIGR00442  94 lPKPFKLYYIGPMFRYERP---QkGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEINSLGILEGRL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 153 AvcgvpesKFRAICSSIDK-LDKMAWKDVRHEMVVKKGLAPEVADRIGDYVQchggvslveqmfQDPRLSQNKQAlEGLG 231
Cdd:TIGR00442 170 E-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------------NAPKILDFLCE-ESRA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 232 DLKLLFEYLTLFGIadKISFDLSLARGLDYYTGVIYEAVLLQTPTQageeplnvGSVAAGGRYDGLVGMFDpkGHKVPCV 311
Cdd:TIGR00442 230 HFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQ--------GSICGGGRYDGLVEELG--GPPTPAV 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 312 GLSIGVERIFYIVEQRmktKGEKVRTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCESTGI 391
Cdd:TIGR00442 298 GFAIGIERLILLLEEL---GLIPPPSKKPDVYVVPLGEEAELEALKLAQKLRKAGIRVEVDLGGR-KLKKQLKYADKLGA 373

                         410       420       430
                  ....*....|....*....|....*....|.
gi 1391723582 392 PLVVIIGEQELKEGVIKIRSVASREEVAIKR 422
Cdd:TIGR00442 374 RFALIIGEDELENGTVTLKDLETGEQETVPL 404
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
 2-421 1.27e-79

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 252.34  E-value: 1.27e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   2 VVREKILDLVISCFKRHGAKGMDTPAFELKETLTEKYG---EDSGLMYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKM 78
Cdd:PRK12420   19 VLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdEILKEIYTLTDQGKRDLALRYDLTIPFAKVVAMNPNIRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  79 --KRYHVGKVWrRESPtIVQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLgDFLIKVNDRRIVDGMFAVCG 156
Cdd:PRK12420   99 pfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVTIQYNNRKLLNGILQAIG 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 157 VPESKFRAICSSIDKLDKMAWKDVRHEmVVKKGLAPEVADRIGDYVQCHGGVSLVEqmFQDPRLSQNKQalEGLGDLKLL 236
Cdd:PRK12420  175 IPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIAD--FKEAFNNPLVA--EGVNELQQL 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 237 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLlqtptqagEEPLNVGSVAAGGRYDGLVGMFDPKGHKVPCVGLSIG 316
Cdd:PRK12420  250 QQYLIALGINENCIFNPFLARGLTMYTGTVYEIFL--------KDGSITSSIGSGGRYDNIIGAFRGDDMNYPTVGISFG 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 317 VERIFYIVEQRmktkgekVRTTETQVFVATPQKNFLQErLKLIAELW-DSGIKAEMLYKNNpKLLTQLHYCESTGIPLVV 395
Cdd:PRK12420  322 LDVIYTALSQK-------ETISSTADVFIIPLGTELQC-LQIAQQLRsTTGLKVELELAGR-KLKKALNYANKENIPYVL 392

                         410       420
                  ....*....|....*....|....*.
gi 1391723582 396 IIGEQELKEGVIKIRSVASREEVAIK 421
Cdd:PRK12420  393 IIGEEEVSTGTVMLRNMKEGSEVKVP 418
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
 4-320 7.48e-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: 163.55  E-value: 7.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   4 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLAmnkvKKMKRYH- 82
Cdd:TIGR00443  11 KEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLVS----TRLRDRPl 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  83 ------VGKVWRRESPTIvqGRYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCG 156
Cdd:TIGR00443  87 plrlcyAGNVFRTNESGG--GRSREFTQAGVELIGA-GGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLEEAG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 157 VPESKFRAICSSIDKLDKMAWKdvrhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEGLGDLKLL 236
Cdd:TIGR00443 164 LPEEAREALREALARKDLVALE----ELVAELGLSPEVRERLLALPRLRGDGEEVLEEAR--ALAGSETAEAALDELEAV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 237 FEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVLlqtpTQAGEeplnvgSVAAGGRYDGLVGMFdpkGHKVPCVGLSIG 316
Cdd:TIGR00443 238 LELLEARGVEEYISLDLGLVRGYHYYTGLIFEGYA----PGLGA------PLAGGGRYDELLGRF---GRPLPATGFALN 304


                  ....
gi 1391723582 317 VERI 320
Cdd:TIGR00443 305 LERL 308
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
4-320 7.51e-45

ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 158.42  E-value: 7.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   4 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQGGELLSLRYDLTVPFARYLA--MNKVKKMKR 80
Cdd:COG3705     8 KEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLqTFKLVDQLGRTLGLRPDMTPQVARIAAtrLANRPGPLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  81 Y-HVGKVWR-RESPtivQGRYREFCQC------DFDIAGqfdpmipDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMF 152
Cdd:COG3705    88 LcYAGNVFRtRPSG---LGRSREFLQAgaeligHAGLEA-------DAEVIALALEALKAAGLEDFTLDLGHVGLFRALL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 153 AVCGVPESKFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdprLSQNKQALEGLGD 232
Cdd:COG3705   158 EALGLSEEQREELRRALARKD---AVELE-ELLAELGLSEELAEALLALPELYGGEEVLARARA---LLLDAAIRAALDE 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 233 LKLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVllqTPTQAGEeplnvgsVAAGGRYDGLVGMFdpkGHKVPCVG 312
Cdd:COG3705   231 LEALAEALAARGPDVRLTFDLSELRGYDYYTGIVFEAY---APGVGDP-------LARGGRYDGLLAAF---GRARPATG 297


                  ....*...
gi 1391723582 313 LSIGVERI 320
Cdd:COG3705   298 FSLDLDRL 305
PLN02530 PLN02530
histidine-tRNA ligase
 24-421 1.64e-42

histidine-tRNA ligase


Pssm-ID: 178145 [Multi-domain]  Cd Length: 487  Bit Score: 156.06  E-value: 1.64e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  24 DTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFARyLAMNKVKKM----KRYHVGKVWRRESPTivQGR 98
Cdd:PLN02530  107 DAPVLESEELYIRKAGEEiTDQLYNFEDKGGRRVALRPELTPSLAR-LVLQKGKSLslplKWFAIGQCWRYERMT--RGR 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  99 YREFCQCDFDIAGqFDPMIPDAECLKIMCEILS--GLQLGDFLIKVNDRRIVDGMFAVCGVPESKFRAICSSIDKLDKMA 176
Cdd:PLN02530  184 RREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKrvGITSSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLP 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 177 WKDVRHEMVvKKGLAPEVADRIGDYVQCHGGVSLVEQMFQDPrlsqnkqalEGLGDLKLLFEYLTLFGIADKISFDLSLA 256
Cdd:PLN02530  263 REEIEKELD-TLGVSEEAIEGILDVLSLKSLDDLEALLGADS---------EAVADLKQLFSLAEAYGYQDWLVFDASVV 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 257 RGLDYYTGVIYEAVllqtpTQAGEeplnVGSVAAGGRYDGLVGMFDpkGHKVPCVGLSIG--VerifyIVEQrMKTKG-- 332
Cdd:PLN02530  333 RGLAYYTGIVFEGF-----DRAGK----LRAICGGGRYDRLLSTFG--GEDTPACGFGFGdaV-----IVEL-LKEKGll 395

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 333 -EKVRTTETQVFvatPQKNFLQ-ERLKLIAELWDSGIKAEMLYKNNpKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIR 410
Cdd:PLN02530  396 pELPHQVDDVVF---ALDEDLQgAAAGVASRLREKGRSVDLVLEPK-KLKWVFKHAERIGAKRLVLVGASEWERGMVRVK 471

                         410
                  ....*....|.
gi 1391723582 411 SVASREEVAIK 421
Cdd:PLN02530  472 DLSSGEQTEVK 482
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
 4-371 3.96e-40

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 147.71  E-value: 3.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   4 REKILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL-MYDLKDQG-GELLSLRYDLTVPFARyLAMNKVKKMKR- 80
Cdd:PRK12292   20 IEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLrTFKLVDQLsGRTLGLRPDMTAQIAR-IAATRLANRPGp 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  81 ----YHvGKVWR---RESptivqGRYREFCQCDFDIAGqFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFA 153
Cdd:PRK12292   99 lrlcYA-GNVFRaqeRGL-----GRSREFLQSGVELIG-DAGLEADAEVILLLLEALKALGLPNFTLDLGHVGLFRALLE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 154 VCGVPESKFRAICSSIDKLDKMAWKdvrhEMVvkKGLAPEVADRIGDYVQCHGGVSLVEQMfqdPRLSQNKQALEGLGDL 233
Cdd:PRK12292  172 AAGLSEELEEVLRRALANKDYVALE----ELV--LDLSEELRDALLALPRLRGGREVLEEA---RKLLPSLPIKRALDEL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 234 KLLFEYLTLFGIADKISFDLSLARGLDYYTGVIYEAVllqtptqAGEEPLNVGSvaaGGRYDGLVGMFdpkGHKVPCVGL 313
Cdd:PRK12292  243 EALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGY-------VDGVGNPIAS---GGRYDDLLGRF---GRARPATGF 309

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1391723582 314 SIGVERifyIVEQRMKTKgekvrTTETQVFVATPQKNFLQERLKLIAELWDSGIKAEM 371
Cdd:PRK12292  310 SLDLDR---LLELQLELP-----VEARKDLVIAPDSEALAAALAAAQELRKKGEIVVL 359
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 3-320 1.29e-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: 138.87  E-value: 1.29e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   3 VREKILDLviscFKRHGAKGMDTPAFELKETLTEKYGEDSGLMYDLKDQGGELLSLRYDLTVPFARYLA--MNKVKKMKR 80
Cdd:pfam13393  16 LRRRLLDL----FRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDAhrLNRPGPLRL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  81 YHVGKVWRRESPTIvqGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPES 160
Cdd:pfam13393  92 CYAGSVLRTRPKGL--GRSREPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALLEAAGLSEA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 161 KFRAICSSIDKLDkmaWKDVRhEMVVKKGLAPEVADRIGDYVQCHGGVSLVEQMFQdpRLSQNKQALEGLGDLKLLFEYL 240
Cdd:pfam13393 169 LEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARA--ALPGLPALQEALDELEALAALL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 241 TLFGIADKISFDLSLARGLDYYTGVIYEAVLLQTPtqageeplnvGSVAAGGRYDGLVGMFdpkGHKVPCVGLSIGVERI 320
Cdd:pfam13393 243 EALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVG----------EPLARGGRYDDLGAAF---GRARPATGFSLDLEAL 309
HisRS_anticodon cd00859
HisRS Histidyl-anticodon binding domain. HisRS belongs to class II aminoacyl-tRNA synthetases ...
 339-430 8.15e-28

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: 105.70  E-value: 8.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 339 ETQVFVATPQKNFLQERLKLIAELWDSGIKAEMLYKNnPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREEV 418
Cdd:cd00859     1 EVDVYVVPLGEGALSEALELAEQLRDAGIKAEIDYGG-RKLKKQFKYADRSGARFAVILGEDELAAGVVTVKDLETGEQE 79

                          90
                  ....*....|..
gi 1391723582 419 AIKRENFVAEIQ 430
Cdd:cd00859    80 TVALDELVEELK 91
syh CHL00201
histidine-tRNA synthetase; Provisional
 7-431 4.50e-26

histidine-tRNA synthetase; Provisional


Pssm-ID: 164576 [Multi-domain]  Cd Length: 430  Bit Score: 109.61  E-value: 4.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   7 ILDLVISCFKRHGAKGMDTPAFELKETLTEKYGEDSGL----MYDLKDQGGELLSLRYDLTVPFARYLAMNKVKKMKR-- 80
Cdd:CHL00201   24 IHDKALTLLSLANYSEIRTPIFENSSLYDRGIGETTDIvnkeMYRFTDRSNRDITLRPEGTAGIVRAFIENKMDYHSNlq 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  81 --YHVGKVWRRESPTivQGRYREFCQCDFDIAGQFDPMiPDAECLKIMCEILSGLQLGDFLIKVN------DRRIVdgmf 152
Cdd:CHL00201  104 rlWYSGPMFRYERPQ--SGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDINsigkleDRQSY---- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 153 avcgvpESKFRAICSSI-DKLDKmawkDVRHEMVVKkglaP-EVADRIGDYVQchggvslvEQMFQDPRLSQ--NKQALE 228
Cdd:CHL00201  177 ------QLKLVEYLSQYqDDLDT----DSQNRLYSN----PiRILDSKNLKTQ--------EILDGAPKISDflSLESTE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 229 GLGDLkllFEYLTLFGIADKISFdlSLARGLDYYTGVIYEavlLQTPTQAGEEplnvgSVAAGGRYDGLVGMFDpkGHKV 308
Cdd:CHL00201  235 HFYDV---CTYLNLLNIPYKINY--KLVRGLDYYNDTAFE---IKTLSSNGQD-----TICGGGRYDSLIHQLG--GPKT 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 309 PCVGLSIGVERIFYIVEQRMKTKGEKVrttetQVFVATPQKNFLQERLKLIAELWDSGIKAEmLYKNNPKLLTQLHYCES 388
Cdd:CHL00201  300 PAVGCAIGLERLLLIAKDNIILPKQSI-----DVYIATQGLKAQKKGWEIIQFLEKQNIKFE-LDLSSSNFHKQIKQAGK 373

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1391723582 389 TGIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQK 431
Cdd:CHL00201  374 KRAKACIILGDNEIMDNCITIKWLDEQVQENAQYSNFKQEISY 416
hisZ PRK12295
ATP phosphoribosyltransferase regulatory subunit; Provisional
 7-320 3.83e-21

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183413 [Multi-domain]  Cd Length: 373  Bit Score: 94.23  E-value: 3.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   7 ILDLVISCFKRHGAKGMDTPAFELKETLTEKYGED-SGLMYDLKDQGGELLSLRYDLTVPFAR-YLAMNKVKKMKRYHVG 84
Cdd:PRK12295   10 AAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDiRRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPARYAYLG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  85 KVWRRESptivqGRYREFCQCDFDIAGQFDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGVPE----- 159
Cdd:PRK12295   90 EVFRQRR-----DRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLPPgwkrr 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 160 --------SKFRAIcssIDKL-------------------DKMAWKDVRHEMVVKKGLAP-------EVADRIGDYVQCH 205
Cdd:PRK12295  165 llrhfgrpRSLDAL---LARLagprvdpldehagvlaalaDEAAARALVEDLMSIAGISPvggrspaEIARRLLEKAALA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 206 GGVSLVEQMFQ--------DPRLSQNKQALEGL-GDLKL-------LFE----YLTLFGIA-DKISFDLSLARGLDYYTG 264
Cdd:PRK12295  242 AAARLPAEALAvlerflaiSGPPDAALAALRALaADAGLdldaaldRFEarlaALAARGIDlERLRFSASFGRPLDYYTG 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1391723582 265 VIYEAvllqTPTQAGEEPLnvgsvAAGGRYDGLVGMFDpKGHKVPCVGLSIGVERI 320
Cdd:PRK12295  322 FVFEI----RAAGNGDPPL-----AGGGRYDGLLTRLG-AGEPIPAVGFSIWLDRL 367
HGTP_anticodon pfam03129
Anticodon binding domain; This domain is found in histidyl, glycyl, threonyl and prolyl tRNA ...
 341-432 2.78e-17

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: 76.47  E-value: 2.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 341 QVFVATPQKN---FLQERLKLIAELWDSGIKAEmLYKNNPKLLTQLHYCESTGIPLVVIIGEQELKEGVIKIRSVASREE 417
Cdd:pfam03129   1 QVVVIPLGEKaeeLEEYAQKLAEELRAAGIRVE-LDDRNESIGKKFRRADLIGIPFALVVGEKELEEGTVTVRRRDTGEQ 79

                          90
                  ....*....|....*
gi 1391723582 418 VAIKRENFVAEIQKR 432
Cdd:pfam03129  80 ETVSLDELVEKLKEL 94
HGTP_anticodon2 pfam12745
Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on ...
 342-432 4.95e-07

Anticodon binding domain of tRNAs; This is an HGTP_anticodon binding domain, found largely on Gcn2 proteins which bind tRNA to down regulate translation in certain stress situations.


Pssm-ID: 432758  Cd Length: 259  Bit Score: 50.68  E-value: 4.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 342 VFVATPQKNFL-QERLKLIAELWDSGIKAEMLYKNNPKLLTQLHYCESTGIPLVVIIGEQEL----KEGVIKIRSVASRE 416
Cdd:pfam12745   8 VLVASFDASILrTTGVEILQELWAHGISADLAVDASYSPEDLVSRARDDGVSWIVIIKQQNKssdsKYKPLKVKNLLRKE 87

                          90       100
                  ....*....|....*....|
gi 1391723582 417 EVAIKRENFVA----EIQKR 432
Cdd:pfam12745  88 DVDLDSDELVSwlrgEIRER 107
PRK12421 PRK12421
ATP phosphoribosyltransferase regulatory subunit; Provisional
 4-320 6.48e-05

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237098  Cd Length: 392  Bit Score: 44.96  E-value: 6.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582   4 REKILDLVIScfkrHGAKGMDTPAFELKETLTEKYGEDSGLM-YDLKDQ-GGELLSLRYDLTVPFARYLA-MNKVKKMKR 80
Cdd:PRK12421   28 RRRLLDLFAS----RGYQLVMPPLIEYLESLLTGAGQDLKLQtFKLIDQlSGRLMGVRADITPQVARIDAhLLNREGVAR 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582  81 Y-HVGKVWRrespTIVQG--RYREFCQCDFDIAGQfDPMIPDAECLKIMCEILSGLQLGDFLIKVNDRRIVDGMFAVCGV 157
Cdd:PRK12421  104 LcYAGSVLH----TLPQGlfGSRTPLQLGAELYGH-AGIEADLEIIRLMLGLLRNAGVPALHLDLGHVGIFRRLAELAGL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 158 PESKFRAIcssidkLDKMAWKDVR--HEMVVKKGLAPEVADRIGDYVQCHGGV-SLVEQMFQDPRlsQNKQALEGLGDLK 234
Cdd:PRK12421  179 SPEEEEEL------FDLLQRKALPelAEVCQNLGVGSDLRRMFYALARLNGGLeALDRALSVLAL--QDAAIRQALDELK 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391723582 235 LLFEYLTLFGIADKISFDLSLARGLDYYTGVIYeAVLLQTPTQAgeeplnvgsVAAGGRYDGLVGMFdpkGHKVPCVGLS 314
Cdd:PRK12421  251 TLAAHLKNRWPELPVSIDLAELRGYHYHTGLVF-AAYIPGRGQA---------LARGGRYDGIGEAF---GRARPATGFS 317


                  ....*.
gi 1391723582 315 IGVERI 320
Cdd:PRK12421  318 MDLKEL 323
ProRS_anticodon_short cd00861
ProRS Prolyl-anticodon binding domain, short version found predominantly in bacteria. ProRS ...
 390-430 6.09e-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: 38.72  E-value: 6.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1391723582 390 GIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQ 430
Cdd:cd00861    54 GIPYRIVVGKKSAAEGIVEIKVRKTGEKEEISIDELLEFLQ 94
PRK09194 PRK09194
prolyl-tRNA synthetase; Provisional
 390-434 5.21e-03

prolyl-tRNA synthetase; Provisional


Pssm-ID: 236405 [Multi-domain]  Cd Length: 565  Bit Score: 38.91  E-value: 5.21e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1391723582 390 GIPLVVIIGEQELKEGVIKIRSVASREEVAIKRENFVAEIQKRLS 434
Cdd:PRK09194  521 GIPHRIVVGDRGLAEGIVEYKDRRTGEKEEVPVDELVEFLKALKK 565
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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