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Conserved domains on  [gi|1712714635|gb|QDV33134|]
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Histidine--tRNA ligase [Tautonia plasticadhaerens]

Protein Classification

HisS family protein( domain architecture ID 1004231)

HisS family protein similar to histidine--tRNA ligase (HisRS), which is responsible for the attachment of histidine to the 3' OH group of ribose of the appropriate tRNA, and ATP phosphoribosyltransferase regulatory subunit (HisZ) that is required for the first step of histidine biosynthesis

CATH:  3.30.930.10|3.40.50.800
SCOP:  4001782|4000507

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HisS super family cl33771
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 19-409 3.47e-68

Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA synthetase is part of the Pathway/BioSystem: Aminoacyl-tRNA synthetases


The actual alignment was detected with superfamily member COG0124:

Pssm-ID: 439894 [Multi-domain]  Cd Length: 422  Bit Score: 221.92  E-value: 3.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  19 VRGTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSK-LFEVAD-GPARLCLRPELTASIV 96
Cdd:COG0124     7 PRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVEKeMYTFEDrGGRSLTLRPEGTAPVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  97 RAFIDTPEAPELPWRVCSSGPVFRYERePGPTRYREFTQAGVELLGAPGPEADAEVIAlaldsaaaagipdasirvghtg 176
Cdd:COG0124    87 RAVAEHGNELPFPFKLYYIGPVFRYER-PQKGRYRQFHQFGVEVIGSDSPLADAEVIA---------------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 177 LIVELLERSGLPSAA--VSSLvehlsdaasegrnvraletaldrlagwlhGDAEQQAEAVLPAIDRADDPGVDRLFrhlv 254
Cdd:COG0124   144 LAADLLKALGLKDFTleINSR-----------------------------GLPEERAEALLRYLDKLDKIGHEDVL---- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 255 prvtgrrtGHEIINRLRRKWALghslgdalgrvrarvhELADLRGPAV-EVLQGLEQGFAALAPGTIRGFLEMLRQLEAR 333
Cdd:COG0124   191 --------DEDSQRRLETNPLR----------------AILDSKGPDCqEVLADAPKLLDYLGEEGLAHFEEVLELLDAL 246

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712714635 334 GIPperVELDLGFGHGIGFYSQMIFELsVSTPSGPLG-ICHGGRYDGLATVLGSDRDPhGVGFAFGVERLYHAIEGL 409
Cdd:COG0124   247 GIP---YVIDPRLVRGLDYYTGTVFEI-VTDGLGAQGsVCGGGRYDGLVEQLGGPPTP-AVGFAIGLERLLLLLEEL 318
 
Name Accession Description Interval E-value
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 19-409 3.47e-68

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: 221.92  E-value: 3.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  19 VRGTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSK-LFEVAD-GPARLCLRPELTASIV 96
Cdd:COG0124     7 PRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVEKeMYTFEDrGGRSLTLRPEGTAPVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  97 RAFIDTPEAPELPWRVCSSGPVFRYERePGPTRYREFTQAGVELLGAPGPEADAEVIAlaldsaaaagipdasirvghtg 176
Cdd:COG0124    87 RAVAEHGNELPFPFKLYYIGPVFRYER-PQKGRYRQFHQFGVEVIGSDSPLADAEVIA---------------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 177 LIVELLERSGLPSAA--VSSLvehlsdaasegrnvraletaldrlagwlhGDAEQQAEAVLPAIDRADDPGVDRLFrhlv 254
Cdd:COG0124   144 LAADLLKALGLKDFTleINSR-----------------------------GLPEERAEALLRYLDKLDKIGHEDVL---- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 255 prvtgrrtGHEIINRLRRKWALghslgdalgrvrarvhELADLRGPAV-EVLQGLEQGFAALAPGTIRGFLEMLRQLEAR 333
Cdd:COG0124   191 --------DEDSQRRLETNPLR----------------AILDSKGPDCqEVLADAPKLLDYLGEEGLAHFEEVLELLDAL 246

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712714635 334 GIPperVELDLGFGHGIGFYSQMIFELsVSTPSGPLG-ICHGGRYDGLATVLGSDRDPhGVGFAFGVERLYHAIEGL 409
Cdd:COG0124   247 GIP---YVIDPRLVRGLDYYTGTVFEI-VTDGLGAQGsVCGGGRYDGLVEQLGGPPTP-AVGFAIGLERLLLLLEEL 318
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
 23-407 8.56e-56

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: 186.28  E-value: 8.56e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  23 RDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAiVSKLFEVADGPAR-LCLRPELTASIVRAFID 101
Cdd:TIGR00443   1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGIL-NEDLFKLFDQLGRvLGLRPDMTAPIARLVST 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 102 TPEAPELPWRVCSSGPVFRYErEPGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGLIVEL 181
Cdd:TIGR00443  80 RLRDRPLPLRLCYAGNVFRTN-ESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 182 LERSGLPsaavsslvehlsdaasegrnvraletaldrlagwlhgdaEQQAEAVLPAIDRADDPGVDRLFRHLvprvtgrr 261
Cdd:TIGR00443 159 LEEAGLP---------------------------------------EEAREALREALARKDLVALEELVAEL-------- 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 262 tgheiinrlrrkwalghslgDALGRVRARVHELADLRGPAVEVLQGLEqgfAALAPGTIRGFLEMLRQ----LEARGiPP 337
Cdd:TIGR00443 192 --------------------GLSPEVRERLLALPRLRGDGEEVLEEAR---ALAGSETAEAALDELEAvlelLEARG-VE 247

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 338 ERVELDLGFGHGIGFYSQMIFElsVSTPSGPLGICHGGRYDGLATVLGSDRdPhGVGFAFGVERLYHAIE 407
Cdd:TIGR00443 248 EYISLDLGLVRGYHYYTGLIFE--GYAPGLGAPLAGGGRYDELLGRFGRPL-P-ATGFALNLERLLEALT 313
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
 21-411 7.49e-48

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 167.74  E-value: 7.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  21 GTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSKLFEVADGPA--RLCLRPELTASIVRA 98
Cdd:PRK12292    8 GIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLRTFKLVDQLSgrTLGLRPDMTAQIARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  99 FIDTPEAPELPWRVCSSGPVFRyEREPGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGLI 178
Cdd:PRK12292   88 AATRLANRPGPLRLCYAGNVFR-AQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDLGHVGLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 179 VELLERSGLPsaavsslvehlsdaasegrnvraletaldrlagwlhgdaEQQAEAVLPAIDRADDPGVDRLFRHLVPrvt 258
Cdd:PRK12292  167 RALLEAAGLS---------------------------------------EELEEVLRRALANKDYVALEELVLDLSE--- 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 259 grrtgheiinrlrrkwalghslgdalgRVRARVHELADLRGPAvEVLQGLEQGFAALAPGTIRGFLEML-RQLEARGiPP 337
Cdd:PRK12292  205 ---------------------------ELRDALLALPRLRGGR-EVLEEARKLLPSLPIKRALDELEALaEALEKYG-YG 255

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712714635 338 ERVELDLGFGHGIGFYSQMIFELSVSTPSGPlgICHGGRYDGLATVLGSDRDphGVGFAFGVERLYHAIEGLRE 411
Cdd:PRK12292  256 IPLSLDLGLLRHLDYYTGIVFEGYVDGVGNP--IASGGRYDDLLGRFGRARP--ATGFSLDLDRLLELQLELPV 325
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 29-407 4.52e-47

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: 162.00  E-value: 4.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  29 DYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSKLFEVAD-GPARLCLRPELTASIVRAFIDTPEAPE 107
Cdd:cd00773     1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSKEMYRFKDkGGRDLALRPDLTAPVARAVAENLLSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 108 LPWRVCSSGPVFRYERePGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGLIVELLERSGL 187
Cdd:cd00773    81 LPLKLYYIGPVFRYER-PQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAGLLED 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 188 PSAAVSSLVEHLSDAASEgrNVRALETALDRLAgwlhgdaeqqaeavlpaidraddpgvdrlfrhlvprvtgrrtgheii 267
Cdd:cd00773   160 REEYIERLIDKLDKEALA--HLEKLLDYLEALG----------------------------------------------- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 268 nrlrrkwalghslgdalgrvrarvheladlrgpavevlqgleqgfaalapgtirgflemlrqleargiPPERVELDLGFG 347
Cdd:cd00773   191 --------------------------------------------------------------------VDIKYSIDLSLV 202

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 348 HGIGFYSQMIFELSVSTPSGPLGICHGGRYDGLATVLGSdRDPHGVGFAFGVERLYHAIE 407
Cdd:cd00773   203 RGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGG-EDVPAVGFAIGLERLLLALE 261
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 21-402 9.88e-41

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: 146.58  E-value: 9.88e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  21 GTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIvSKLFEVADGPAR-LCLRPELTASIVRAF 99
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADL-DQTFKLVDQSGRlLGLRADITPQVARID 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 100 IDTPEAPElPWRVCSSGPVFRyEREPGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGLIV 179
Cdd:pfam13393  80 AHRLNRPG-PLRLCYAGSVLR-TRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 180 ELLERSGLPSAAVSSLVEHLSDAASEgrnvraletALDRLAGWLHGDAEQqaeavlpaidraddpgvdrlfRHLVPRVTG 259
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKDAA---------ELAELAAEAGLPPAL---------------------RRALLALPD 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 260 RRTGHEIINRLRRKWALGHSLGDALGRVRarvheladlrgpavevlqgleqgfaalapgtirgflEMLRQLEARGiPPER 339
Cdd:pfam13393 208 LYGGPEVLDEARAALPGLPALQEALDELE------------------------------------ALAALLEALG-DGVR 250

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712714635 340 VELDLGFGHGIGFYSQMIFELSVSTPSGPLGicHGGRYDGLATVLGSDRDphGVGFAFGVERL 402
Cdd:pfam13393 251 LTFDLAELRGYEYYTGIVFAAYAPGVGEPLA--RGGRYDDLGAAFGRARP--ATGFSLDLEAL 309
 
Name Accession Description Interval E-value
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 19-409 3.47e-68

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: 221.92  E-value: 3.47e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  19 VRGTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSK-LFEVAD-GPARLCLRPELTASIV 96
Cdd:COG0124     7 PRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGEDIVEKeMYTFEDrGGRSLTLRPEGTAPVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  97 RAFIDTPEAPELPWRVCSSGPVFRYERePGPTRYREFTQAGVELLGAPGPEADAEVIAlaldsaaaagipdasirvghtg 176
Cdd:COG0124    87 RAVAEHGNELPFPFKLYYIGPVFRYER-PQKGRYRQFHQFGVEVIGSDSPLADAEVIA---------------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 177 LIVELLERSGLPSAA--VSSLvehlsdaasegrnvraletaldrlagwlhGDAEQQAEAVLPAIDRADDPGVDRLFrhlv 254
Cdd:COG0124   144 LAADLLKALGLKDFTleINSR-----------------------------GLPEERAEALLRYLDKLDKIGHEDVL---- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 255 prvtgrrtGHEIINRLRRKWALghslgdalgrvrarvhELADLRGPAV-EVLQGLEQGFAALAPGTIRGFLEMLRQLEAR 333
Cdd:COG0124   191 --------DEDSQRRLETNPLR----------------AILDSKGPDCqEVLADAPKLLDYLGEEGLAHFEEVLELLDAL 246

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1712714635 334 GIPperVELDLGFGHGIGFYSQMIFELsVSTPSGPLG-ICHGGRYDGLATVLGSDRDPhGVGFAFGVERLYHAIEGL 409
Cdd:COG0124   247 GIP---YVIDPRLVRGLDYYTGTVFEI-VTDGLGAQGsVCGGGRYDGLVEQLGGPPTP-AVGFAIGLERLLLLLEEL 318
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
 23-407 8.56e-56

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: 186.28  E-value: 8.56e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  23 RDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAiVSKLFEVADGPAR-LCLRPELTASIVRAFID 101
Cdd:TIGR00443   1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGIL-NEDLFKLFDQLGRvLGLRPDMTAPIARLVST 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 102 TPEAPELPWRVCSSGPVFRYErEPGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGLIVEL 181
Cdd:TIGR00443  80 RLRDRPLPLRLCYAGNVFRTN-ESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 182 LERSGLPsaavsslvehlsdaasegrnvraletaldrlagwlhgdaEQQAEAVLPAIDRADDPGVDRLFRHLvprvtgrr 261
Cdd:TIGR00443 159 LEEAGLP---------------------------------------EEAREALREALARKDLVALEELVAEL-------- 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 262 tgheiinrlrrkwalghslgDALGRVRARVHELADLRGPAVEVLQGLEqgfAALAPGTIRGFLEMLRQ----LEARGiPP 337
Cdd:TIGR00443 192 --------------------GLSPEVRERLLALPRLRGDGEEVLEEAR---ALAGSETAEAALDELEAvlelLEARG-VE 247

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 338 ERVELDLGFGHGIGFYSQMIFElsVSTPSGPLGICHGGRYDGLATVLGSDRdPhGVGFAFGVERLYHAIE 407
Cdd:TIGR00443 248 EYISLDLGLVRGYHYYTGLIFE--GYAPGLGAPLAGGGRYDELLGRFGRPL-P-ATGFALNLERLLEALT 313
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 19-409 1.73e-54

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: 185.76  E-value: 1.73e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  19 VRGTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAA--IVSK-LFEVAD-GPARLCLRPELTAS 94
Cdd:TIGR00442   3 PRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVGEEtdIVSKeMYTFKDkGGRSLTLRPEGTAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  95 IVRAFIDTPEAPELPWRVCSSGPVFRYERePGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGH 174
Cdd:TIGR00442  83 VARAVIENKLLLPKPFKLYYIGPMFRYER-PQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTLEINS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 175 TGLIVELLErsglpsaavssLVEHLsdaasegrnVRALETALDRLagwlhgdaeqqaeavlpaidraDDPGVDRLFRhlv 254
Cdd:TIGR00442 162 LGILEGRLE-----------YREAL---------IRYLDKHKDKL----------------------GEDSVRRLEK--- 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 255 prvtgrrtgheiiNRLRrkwalghSLGDALGRVRarvheladlrgpavEVLQGLEQGFAALAPGTIRGFLEMLRQLEARG 334
Cdd:TIGR00442 197 -------------NPLR-------ILDSKNEKIQ--------------ELLKNAPKILDFLCEESRAHFEELKELLDALG 242

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712714635 335 IPperVELDLGFGHGIGFYSQMIFELsVSTPSGPLG-ICHGGRYDGLATVLGSDRDPhGVGFAFGVERLYHAIEGL 409
Cdd:TIGR00442 243 IP---YKIDPSLVRGLDYYTGTVFEF-VTDDLGAQGsICGGGRYDGLVEELGGPPTP-AVGFAIGIERLILLLEEL 313
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
26-408 1.92e-52

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


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 177.68  E-value: 1.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  26 LPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSKLFEVADGPAR-LCLRPELTASIVRAFIDTPE 104
Cdd:COG3705     1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLLTGSGADLDLQTFKLVDQLGRtLGLRPDMTPQVARIAATRLA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 105 APELPWRVCSSGPVFRYeREPGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGLIVELLER 184
Cdd:COG3705    81 NRPGPLRLCYAGNVFRT-RPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 185 SGLPsaavsslvehlsdaasegrnvraletaldrlagwlhgdaEQQAEAVLPAIDRADDPGVDRLFRhlvprvtgrrtgh 264
Cdd:COG3705   160 LGLS---------------------------------------EEQREELRRALARKDAVELEELLA------------- 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 265 eiinrlrrkwalGHSLGDALgrvRARVHELADLRGPAvEVLQGLEqgfAALAPGTIRGFLEMLRQ----LEARGiPPERV 340
Cdd:COG3705   188 ------------ELGLSEEL---AEALLALPELYGGE-EVLARAR---ALLLDAAIRAALDELEAlaeaLAARG-PDVRL 247

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1712714635 341 ELDLGFGHGIGFYSQMIFELSVSTPSGPLGicHGGRYDGLATVLGSDRdPhGVGFAFGVERLYHAIEG 408
Cdd:COG3705   248 TFDLSELRGYDYYTGIVFEAYAPGVGDPLA--RGGRYDGLLAAFGRAR-P-ATGFSLDLDRLLRALPA 311
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
 21-411 7.49e-48

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 167.74  E-value: 7.49e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  21 GTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSKLFEVADGPA--RLCLRPELTASIVRA 98
Cdd:PRK12292    8 GIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGAILDLRTFKLVDQLSgrTLGLRPDMTAQIARI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  99 FIDTPEAPELPWRVCSSGPVFRyEREPGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGLI 178
Cdd:PRK12292   88 AATRLANRPGPLRLCYAGNVFR-AQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDLGHVGLF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 179 VELLERSGLPsaavsslvehlsdaasegrnvraletaldrlagwlhgdaEQQAEAVLPAIDRADDPGVDRLFRHLVPrvt 258
Cdd:PRK12292  167 RALLEAAGLS---------------------------------------EELEEVLRRALANKDYVALEELVLDLSE--- 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 259 grrtgheiinrlrrkwalghslgdalgRVRARVHELADLRGPAvEVLQGLEQGFAALAPGTIRGFLEML-RQLEARGiPP 337
Cdd:PRK12292  205 ---------------------------ELRDALLALPRLRGGR-EVLEEARKLLPSLPIKRALDELEALaEALEKYG-YG 255

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712714635 338 ERVELDLGFGHGIGFYSQMIFELSVSTPSGPlgICHGGRYDGLATVLGSDRDphGVGFAFGVERLYHAIEGLRE 411
Cdd:PRK12292  256 IPLSLDLGLLRHLDYYTGIVFEGYVDGVGNP--IASGGRYDDLLGRFGRARP--ATGFSLDLDRLLELQLELPV 325
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 29-407 4.52e-47

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: 162.00  E-value: 4.52e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  29 DYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSKLFEVAD-GPARLCLRPELTASIVRAFIDTPEAPE 107
Cdd:cd00773     1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEVSKEMYRFKDkGGRDLALRPDLTAPVARAVAENLLSLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 108 LPWRVCSSGPVFRYERePGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGLIVELLERSGL 187
Cdd:cd00773    81 LPLKLYYIGPVFRYER-PQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAGLLED 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 188 PSAAVSSLVEHLSDAASEgrNVRALETALDRLAgwlhgdaeqqaeavlpaidraddpgvdrlfrhlvprvtgrrtgheii 267
Cdd:cd00773   160 REEYIERLIDKLDKEALA--HLEKLLDYLEALG----------------------------------------------- 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 268 nrlrrkwalghslgdalgrvrarvheladlrgpavevlqgleqgfaalapgtirgflemlrqleargiPPERVELDLGFG 347
Cdd:cd00773   191 --------------------------------------------------------------------VDIKYSIDLSLV 202

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 348 HGIGFYSQMIFELSVSTPSGPLGICHGGRYDGLATVLGSdRDPHGVGFAFGVERLYHAIE 407
Cdd:cd00773   203 RGLDYYTGIVFEAVADGLGAQGSIAGGGRYDGLLEEFGG-EDVPAVGFAIGLERLLLALE 261
hisZ PRK12295
ATP phosphoribosyltransferase regulatory subunit; Provisional
 31-408 1.44e-43

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183413 [Multi-domain]  Cd Length: 373  Bit Score: 155.86  E-value: 1.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  31 AAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSKLFEVAD-GPARLCLRPELTASIVRAFIDTpeAPELP 109
Cdd:PRK12295    5 SASAAAAEALLASFEAAGAVRVDPPILQPAEPFLDLSGEDIRRRIFVTSDeNGEELCLRPDFTIPVCRRHIAT--AGGEP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 110 WRVCSSGPVFRYEREpgptRYREFTQAGVELLGAPGPE-ADAEVIALALDSAAAAGIPDASIRVGHTGLIVELLERSGLP 188
Cdd:PRK12295   83 ARYAYLGEVFRQRRD----RASEFLQAGIESFGRADPAaADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 189 SAAVSSLVEHLSDAasegrnvRALETALDRLAGWLhGDAEQQAEAVLPAIdrADDPGVDRLFRHL-----VPRVTGRRTG 263
Cdd:PRK12295  159 PGWKRRLLRHFGRP-------RSLDALLARLAGPR-VDPLDEHAGVLAAL--ADEAAARALVEDLmsiagISPVGGRSPA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 264 hEIINRLRRKWAL--GHSLGDAlgrVRARVHELADLRGPAVEVLQGLEqGFAALAPGTIRGFLEMLRQ----LEARGIPP 337
Cdd:PRK12295  229 -EIARRLLEKAALaaAARLPAE---ALAVLERFLAISGPPDAALAALR-ALAADAGLDLDAALDRFEArlaaLAARGIDL 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1712714635 338 ERVELDLGFGHGIGFYSQMIFELSVSTPSGPLgICHGGRYDGLATVLGSDRDPHGVGFAFGVERLYHAIEG 408
Cdd:PRK12295  304 ERLRFSASFGRPLDYYTGFVFEIRAAGNGDPP-LAGGGRYDGLLTRLGAGEPIPAVGFSIWLDRLAALGGA 373
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 21-402 9.88e-41

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: 146.58  E-value: 9.88e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  21 GTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIvSKLFEVADGPAR-LCLRPELTASIVRAF 99
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADL-DQTFKLVDQSGRlLGLRADITPQVARID 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 100 IDTPEAPElPWRVCSSGPVFRyEREPGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGLIV 179
Cdd:pfam13393  80 AHRLNRPG-PLRLCYAGSVLR-TRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 180 ELLERSGLPSAAVSSLVEHLSDAASEgrnvraletALDRLAGWLHGDAEQqaeavlpaidraddpgvdrlfRHLVPRVTG 259
Cdd:pfam13393 158 ALLEAAGLSEALEEALRAALQRKDAA---------ELAELAAEAGLPPAL---------------------RRALLALPD 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 260 RRTGHEIINRLRRKWALGHSLGDALGRVRarvheladlrgpavevlqgleqgfaalapgtirgflEMLRQLEARGiPPER 339
Cdd:pfam13393 208 LYGGPEVLDEARAALPGLPALQEALDELE------------------------------------ALAALLEALG-DGVR 250

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1712714635 340 VELDLGFGHGIGFYSQMIFELSVSTPSGPLGicHGGRYDGLATVLGSDRDphGVGFAFGVERL 402
Cdd:pfam13393 251 LTFDLAELRGYEYYTGIVFAAYAPGVGEPLA--RGGRYDDLGAAFGRARP--ATGFSLDLEAL 309
syh CHL00201
histidine-tRNA synthetase; Provisional
 14-407 6.77e-22

histidine-tRNA synthetase; Provisional


Pssm-ID: 164576 [Multi-domain]  Cd Length: 430  Bit Score: 96.89  E-value: 6.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  14 APIPQVRGTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSG--AAIVSK-LFEVADGPAR-LCLRP 89
Cdd:CHL00201    2 AKIQAIRGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFENSSLYDRGIGetTDIVNKeMYRFTDRSNRdITLRP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  90 ELTASIVRAFIDTpeapELPW-----RVCSSGPVFRYERePGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAG 164
Cdd:CHL00201   82 EGTAGIVRAFIEN----KMDYhsnlqRLWYSGPMFRYER-PQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQ 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 165 IPDASIRVGHTGlivELLERSGLPsaavSSLVEHLSDaasegrnvraletaldrlagwLHGDAEQQAEavlpaidraddp 244
Cdd:CHL00201  157 VKNLILDINSIG---KLEDRQSYQ----LKLVEYLSQ---------------------YQDDLDTDSQ------------ 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 245 gvDRLFRHLVPRVTGRRTGHEIInrlrrkwalghsLGDAlgrvrARVHELADLRGpavevlqglEQGFaalapGTIRGFL 324
Cdd:CHL00201  197 --NRLYSNPIRILDSKNLKTQEI------------LDGA-----PKISDFLSLES---------TEHF-----YDVCTYL 243

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 325 EMLrqlearGIPperVELDLGFGHGIGFYSQMIFELSVSTPSGPLGICHGGRYDGLATVLGSDRDPhGVGFAFGVERLYH 404
Cdd:CHL00201  244 NLL------NIP---YKINYKLVRGLDYYNDTAFEIKTLSSNGQDTICGGGRYDSLIHQLGGPKTP-AVGCAIGLERLLL 313


                  ...
gi 1712714635 405 AIE 407
Cdd:CHL00201  314 IAK 316
PLN02530 PLN02530
histidine-tRNA ligase
 6-398 4.20e-21

histidine-tRNA ligase


Pssm-ID: 178145 [Multi-domain]  Cd Length: 487  Bit Score: 95.19  E-value: 4.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635   6 PGTPTQREAPIPQV-----RGTRDWLPDDYaaiaSLERSLMDRFAAS----GFRPVKTPILEGTELHERKSGAAIVSKLF 76
Cdd:PLN02530   55 TAPPSVQEDGKPKIdvnppKGTRDFPPEDM----RLRNWLFDHFREVsrlfGFEEVDAPVLESEELYIRKAGEEITDQLY 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  77 EVAD-GPARLCLRPELTASIVRAFIDTPEAPELPWRVCSSGPVFRYER-EPGptRYREFTQAGVELLGAPGPEADAEVIA 154
Cdd:PLN02530  131 NFEDkGGRRVALRPELTPSLARLVLQKGKSLSLPLKWFAIGQCWRYERmTRG--RRREHYQWNMDIIGVPGVEAEAELLA 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 155 LaldsaaaagipdasirvghtglIVELLERSGLPSAAVSSLVehlsdaasEGRNVraLETALDRLagwlhGDAEQQAEAV 234
Cdd:PLN02530  209 A----------------------IVTFFKRVGITSSDVGIKV--------SSRKV--LQAVLKSY-----GIPEESFAPV 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 235 LPAIDRADDPGVDRLFRHLVPRVTGRRTGHEIINRLRRKwalghslgdalgrvraRVHELADLRGPAVEVLQGLEQGFaA 314
Cdd:PLN02530  252 CVIVDKLEKLPREEIEKELDTLGVSEEAIEGILDVLSLK----------------SLDDLEALLGADSEAVADLKQLF-S 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 315 LApgtirgflemlrqlEARGIpPERVELDLGFGHGIGFYSQMIFElsVSTPSGPL-GICHGGRYDGLATVLGSDRDPhGV 393
Cdd:PLN02530  315 LA--------------EAYGY-QDWLVFDASVVRGLAYYTGIVFE--GFDRAGKLrAICGGGRYDRLLSTFGGEDTP-AC 376


                  ....*
gi 1712714635 394 GFAFG 398
Cdd:PLN02530  377 GFGFG 381
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
 19-407 4.25e-20

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 91.72  E-value: 4.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  19 VRGTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERK--SGAAIVSKLFEVADGPAR-LCLRPELTASI 95
Cdd:PRK12420    7 VKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKygGGDEILKEIYTLTDQGKRdLALRYDLTIPF 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  96 VRAFIDTPEApELPWRVCSSGPVFRyerePGPT---RYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPdASIRV 172
Cdd:PRK12420   87 AKVVAMNPNI-RLPFKRYEIGKVFR----DGPIkqgRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNLE-VTIQY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 173 GHTGLIVELLERSGLPsaavsslvehlsdaasegrnvraletaldrlagwlhgdaEQQAEAVLPAIDRADDPGVDRLFRH 252
Cdd:PRK12420  161 NNRKLLNGILQAIGIP---------------------------------------TELTSDVILSLDKIEKIGIDGVRKD 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 253 LVPRVTGRRTGHEIINRLRrkwalghsLGDALGRVRARVHELADLRGPAVEVLQGLEQGFAALAPGTIRGFLEMLrqleA 332
Cdd:PRK12420  202 LLERGISEEMADTICNTVL--------SCLQLSIADFKEAFNNPLVAEGVNELQQLQQYLIALGINENCIFNPFL----A 269

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1712714635 333 RgipperveldlgfghGIGFYSQMIFELSVSTPSGPLGICHGGRYDG-LATVLGSDRDPHGVGFAFGVERLYHAIE 407
Cdd:PRK12420  270 R---------------GLTMYTGTVYEIFLKDGSITSSIGSGGRYDNiIGAFRGDDMNYPTVGISFGLDVIYTALS 330
PLN02972 PLN02972
Histidyl-tRNA synthetase
 8-411 6.71e-14

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 73.77  E-value: 6.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635   8 TPTQREAP-IPqvRGTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAivSKL-FEVADGPARL 85
Cdd:PLN02972  320 SNEVRRLPkIP--KGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKYGED--SKLiYDLADQGGEL 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  86 C-LRPELTASIVRAFIdtpeapelpwrVCSSGPVFRYE-----REPGPT--RYREFTQAGVELLGAPGP-EADAEVIALA 156
Cdd:PLN02972  396 CsLRYDLTVPFARYVA-----------MNGITSFKRYQiakvyRRDNPSkgRYREFYQCDFDIAGVYEPmGPDFEIIKVL 464

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 157 LDSAAAAGIPDASIRVGHTGLIVELLERSGLPSaavsslvehlsdaasegrnvraletaldrlagwlhgdaeQQAEAVLP 236
Cdd:PLN02972  465 TELLDELDIGTYEVKLNHRKLLDGMLEICGVPP---------------------------------------EKFRTICS 505

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 237 AIDRADDPGVDRLFRHLVprvtgrrtgheiinrlrRKWALGHSLGDALGRvrarvheLADLRGPAVEVLQGLEQGFAALA 316
Cdd:PLN02972  506 SIDKLDKQSFEQVKKEMV-----------------EEKGLSNETADKIGN-------FVKERGPPLELLSKLRQEGSEFL 561

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635 317 --PGTIRGFLE---MLRQLEARGIPpERVELDLGFGHGIGFYSQMIFElSVSTPSGPLGICHGGRYDGLATVLGSDRDPh 391
Cdd:PLN02972  562 gnASSRAALDEleiMFKALEKSKAI-GKIVFDLSLARGLDYYTGVIYE-AVFKGAQVGSIAAGGRYDNLVGMFSGKQVP- 638

                         410       420
                  ....*....|....*....|
gi 1712714635 392 GVGFAFGVERLYHAIEGLRE 411
Cdd:PLN02972  639 AVGVSLGIERVFAIMEQQEE 658
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 ...
 36-153 1.85e-13

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: 69.34  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  36 LERSLMDRFAASGFRPVKTPILEGTELHErKSGA--AIVSKLFEVADGPAR-----LCLRPELTASIVRAFID-TPEAPE 107
Cdd:cd00670     8 LERFLDDRMAEYGYQEILFPFLAPTVLFF-KGGHldGYRKEMYTFEDKGRElrdtdLVLRPAACEPIYQIFSGeILSYRA 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1712714635 108 LPWRVCSSGPVFRYEREP--GPTRYREFTQAGVELLGAPG--PEADAEVI 153
Cdd:cd00670    87 LPLRLDQIGPCFRHEPSGrrGLMRVREFRQVEYVVFGEPEeaEEERREWL 136
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 33-151 2.17e-13

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: 68.68  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  33 IASLERSLMDRFAASGFRPVKTPILEGTELhERKSGAAIVSKLFEVADGPARLCLRPELTASIVRAFIDTPEApeLPWRV 112
Cdd:cd00768     2 RSKIEQKLRRFMAELGFQEVETPIVEREPL-LEKAGHEPKDLLPVGAENEEDLYLRPTLEPGLVRLFVSHIRK--LPLRL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1712714635 113 CSSGPVFRYEREP-GPTRYREFTQAGVELLGAPGPEADAE 151
Cdd:cd00768    79 AEIGPAFRNEGGRrGLRRVREFTQLEGEVFGEDGEEASEF 118
PRK12421 PRK12421
ATP phosphoribosyltransferase regulatory subunit; Provisional
 21-241 4.38e-11

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237098  Cd Length: 392  Bit Score: 64.22  E-value: 4.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  21 GTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIVSKLFEVADG-PARLC-LRPELTASIVRa 98
Cdd:PRK12421   12 GVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLLTGAGQDLKLQTFKLIDQlSGRLMgVRADITPQVAR- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  99 fIDTPEAP-ELPWRVCSSGPVFRyEREPGPTRYREFTQAGVELLGAPGPEADAEVIALALDSAAAAGIPDASIRVGHTGL 177
Cdd:PRK12421   91 -IDAHLLNrEGVARLCYAGSVLH-TLPQGLFGSRTPLQLGAELYGHAGIEADLEIIRLMLGLLRNAGVPALHLDLGHVGI 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1712714635 178 IVELLERSGLPSAAVSSLVEHLS-------DAASEGRNV-RALETALDRLAGwLHGDAE--QQAEAVLPAIDRA 241
Cdd:PRK12421  169 FRRLAELAGLSPEEEEELFDLLQrkalpelAEVCQNLGVgSDLRRMFYALAR-LNGGLEalDRALSVLALQDAA 241
tRNA-synt_2b pfam00587
tRNA synthetase class II core domain (G, H, P, S and T); tRNA-synt_2b is a family of largely ...
 80-153 2.00e-06

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: 47.79  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  80 DGPARLCLRPELTASIVRAFIDTPEAPE-LPWRVCSSGPVFRYEREP---GPTRYREFTQAGVELLGAPG--PEADAEVI 153
Cdd:pfam00587   6 ENGDELALKPTNEPGHTLLFREEGLRSKdLPLKLAQFGTCFRHEASGdtrGLIRVRQFHQDDAHIFHAPGqsPDELEDYI 85
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 4-345 2.33e-03

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 40.24  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635    4 PPPGTPTQREAPIPQVRGTRDWLPDDYAAIASLERSLMDRFAASGFRPVKTPILEGTELHERKSGAAIV---SKLFEVAD 80
Cdd:COG3321    862 PLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLalvALAAAAAA 941

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635   81 GPARLCLRPELTASIVRAFIDTPEAPELPWRVCSSGPVFRYEREPGPTRYREFTQAGVELLGAPGPEADAEVIALALDSA 160
Cdd:COG3321    942 LLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAAL 1021

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  161 AAAGIPDASIRVGHTGLIVELLERSGLPSAAVSSLVEHLSDAASEGRNVRALETALDRLAGWLHGDAEQQAEAVLPAIDR 240
Cdd:COG3321   1022 LALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALALALAA 1101

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1712714635  241 ADDPGVDRLFRHLVPRVTGRRTGHEIINRLRRkwALGHSLGDALGRVRARVHELADLRGPAVEVLQGLEQGFAALAPGTI 320
Cdd:COG3321   1102 LAAALLLLALLAALALAAAAAALLALAALLAA--AAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALAL 1179

                          330       340
                   ....*....|....*....|....*
gi 1712714635  321 RGFLEMLRQLEARGIPPERVELDLG 345
Cdd:COG3321   1180 ALAAALAAALAGLAALLLAALLAAL 1204
 
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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