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Conserved domains on  [gi|642099577|emb|CDQ77432|]
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unnamed protein product [Oncorhynchus mykiss]

Protein Classification

histidine--tRNA ligase( domain architecture ID 12908282)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02972 super family cl33611
Histidyl-tRNA synthetase
 57-333 5.33e-131

Histidyl-tRNA synthetase


The actual alignment was detected with superfamily member PLN02972:

Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 394.64  E-value: 5.33e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  57 KTAKGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGK---TLSFIYDLKDQGGELLSLRYDLTVPFA 133
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKygeDSKLIYDLADQGGELCSLRYDLTVPFA 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 134 RYLAMNKITNIKRYHIAKVYCRDNPamTRGRYREFYQCDFDIAGQYDPMIPDAECLKIVHEILSDLELGDFRIKVNDKRI 213
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 214 LDGMFAVCGVPDDKFRTICSTVDKLDKMSWEDVKSEMVNEKGLSEEAADQIGQYVSMQGG-MDLAERLLQ-DAKMSQSKQ 291
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 642099577 292 ACAGLTDMKQLFSYLQLFQVTDKVVFDLSLA----HYTGVIYEAIL 333
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLArgldYYTGVIYEAVF 611
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 5-49 3.05e-19

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


:

Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 80.59  E-value: 3.05e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 642099577   5 AQIQDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQIGGDE 49
Cdd:cd00938    1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 57-333 5.33e-131

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 394.64  E-value: 5.33e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  57 KTAKGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGK---TLSFIYDLKDQGGELLSLRYDLTVPFA 133
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKygeDSKLIYDLADQGGELCSLRYDLTVPFA 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 134 RYLAMNKITNIKRYHIAKVYCRDNPamTRGRYREFYQCDFDIAGQYDPMIPDAECLKIVHEILSDLELGDFRIKVNDKRI 213
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 214 LDGMFAVCGVPDDKFRTICSTVDKLDKMSWEDVKSEMVNEKGLSEEAADQIGQYVSMQGG-MDLAERLLQ-DAKMSQSKQ 291
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 642099577 292 ACAGLTDMKQLFSYLQLFQVTDKVVFDLSLA----HYTGVIYEAIL 333
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLArgldYYTGVIYEAVF 611
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 69-335 1.72e-74

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: 233.26  E-value: 1.72e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  69 QMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGKTLSF----IYDLKDQGGELLSLRYDLTVPFARYLAMNKI--- 141
Cdd:cd00773    1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvskeMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 142 TNIKRYHIAKVYCRDNPAmtRGRYREFYQCDFDIAGqYDPMIPDAECLKIVHEILSDLELGDFRIKVNDKRILDGmfaVC 221
Cdd:cd00773   81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 222 GVPDDKFRTICSTVDKLDKmswedvksemvnekglseeaadqigqyvsmqggmdlaerllqdakmsqskqacAGLTDMKQ 301
Cdd:cd00773  155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 642099577 302 LFSYLQLFQVTDKVVFDLSLA----HYTGVIYEAILTQ 335
Cdd:cd00773  182 LLDYLEALGVDIKYSIDLSLVrgldYYTGIVFEAVADG 219
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 55-337 3.76e-56

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: 190.72  E-value: 3.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  55 TLKTAKGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGKT-------LsfIYDLKDQGGELLSLRYD 127
Cdd:COG0124    3 KIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIgedivekE--MYTFEDRGGRSLTLRPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 128 LTVPFARYLAMNKITN---IKRYHIAKVYCRDNPAmtRGRYREFYQCDFDIAGQYDPMIpDAECLKIVHEILSDLELGDF 204
Cdd:COG0124   81 GTAPVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 205 RIKVNDkRildgmfavcGVPDDKFRTICSTVDKLDKMSWEDVksemvnekgLSEEAADQIGQYV----------SMQGGM 274
Cdd:COG0124  158 TLEINS-R---------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLETNPlraildskgpDCQEVL 218

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 642099577 275 DLAERLLQDAKMsqskqacAGLTDMKQLFSYLQLFQVtdKVVFDLSLAH----YTGVIYEAILTQNG 337
Cdd:COG0124  219 ADAPKLLDYLGE-------EGLAHFEEVLELLDALGI--PYVIDPRLVRgldyYTGTVFEIVTDGLG 276
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 60-337 7.11e-52

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: 178.83  E-value: 7.11e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577   60 KGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGKT-------LSFIYDLKDQGGELLSLRYDLTVPF 132
Cdd:TIGR00442   4 RGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVgeetdivSKEMYTFKDKGGRSLTLRPEGTAPV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  133 ARYLAMNKITN---IKRYHIAKVYCRDNPAmtRGRYREFYQCDFDIAGQYDPMIpDAECLKIVHEILSDLELGDFRIKVN 209
Cdd:TIGR00442  84 ARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  210 DKRILDGMFAvcgvpddKFRTICSTVDK-LDKMSWEDVKSEMVNEKGLSEEAADQIGQYVSmqggmdLAERLLQDAKMsq 288
Cdd:TIGR00442 161 SLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------NAPKILDFLCE-- 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 642099577  289 skqacAGLTDMKQLFSYLQLFQVtdKVVFDLSLA----HYTGVIYEAILTQNG 337
Cdd:TIGR00442 226 -----ESRAHFEELKELLDALGI--PYKIDPSLVrgldYYTGTVFEFVTDDLG 271
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 61-331 8.18e-27

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: 109.21  E-value: 8.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577   61 GTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETL---TGKTLSFIYDLKDQGGELLSLRYDLTVPFARYLA 137
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLltgTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  138 mnkiTNIKRYHIAKV-YC----RDNPAMTRGRyREFYQCDFDIAGQYDPMiPDAECLKIVHEILSDLELGDFRIKVNDKR 212
Cdd:pfam13393  81 ----HRLNRPGPLRLcYAgsvlRTRPKGLGRS-REPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  213 ILDGMFAVCGVPDDKFRTICSTVDKLDkmsWEDVKsEMVNEKGLSEEAADQIGQYVSMQGGMDLAERLLQDakMSQSKQA 292
Cdd:pfam13393 155 LVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPAL 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 642099577  293 CAGLTDMKQLFSYLQLFQVTDKVVFDLSLAH----YTGVIYEA 331
Cdd:pfam13393 229 QEALDELEALAALLEALGDGVRLTFDLAELRgyeyYTGIVFAA 271
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 5-49 3.05e-19

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 80.59  E-value: 3.05e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 642099577   5 AQIQDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQIGGDE 49
Cdd:cd00938    1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
WHEP-TRS pfam00458
WHEP-TRS domain;
7-69 1.96e-15

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 69.83  E-value: 1.96e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 642099577    7 IQDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQiggdegkhqftLKTAKGTrDYNPKQ 69
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQ-----------YKALTGK-DYKPGA 51
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 8-51 8.45e-14

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 65.44  E-value: 8.45e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 642099577     8 QDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQIGGDEGK 51
Cdd:smart00991   1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQ 44
PLN02734 PLN02734
glycyl-tRNA synthetase
 5-88 9.87e-06

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 47.82  E-value: 9.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577   5 AQIQDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQIGGDEgKHQFTLKTAKGTRDYNPKqmAIRERVFNTIIR-- 82
Cdd:PLN02734  10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALE-KELQAAVGAGGDGAASKE--AFRQAVVNTLERrl 86

                         90
                 ....*....|
gi 642099577  83 ----CFKHHG 88
Cdd:PLN02734  87 fyipSFKIYG 96
 
Name Accession Description Interval E-value
PLN02972 PLN02972
Histidyl-tRNA synthetase
 57-333 5.33e-131

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 394.64  E-value: 5.33e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  57 KTAKGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGK---TLSFIYDLKDQGGELLSLRYDLTVPFA 133
Cdd:PLN02972 328 KIPKGTRDFAKEQMAIREKAFSIITSVFKRHGATALDTPVFELRETLMGKygeDSKLIYDLADQGGELCSLRYDLTVPFA 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 134 RYLAMNKITNIKRYHIAKVYCRDNPamTRGRYREFYQCDFDIAGQYDPMIPDAECLKIVHEILSDLELGDFRIKVNDKRI 213
Cdd:PLN02972 408 RYVAMNGITSFKRYQIAKVYRRDNP--SKGRYREFYQCDFDIAGVYEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKL 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 214 LDGMFAVCGVPDDKFRTICSTVDKLDKMSWEDVKSEMVNEKGLSEEAADQIGQYVSMQGG-MDLAERLLQ-DAKMSQSKQ 291
Cdd:PLN02972 486 LDGMLEICGVPPEKFRTICSSIDKLDKQSFEQVKKEMVEEKGLSNETADKIGNFVKERGPpLELLSKLRQeGSEFLGNAS 565

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 642099577 292 ACAGLTDMKQLFSYLQLFQVTDKVVFDLSLA----HYTGVIYEAIL 333
Cdd:PLN02972 566 SRAALDELEIMFKALEKSKAIGKIVFDLSLArgldYYTGVIYEAVF 611
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
 69-335 1.72e-74

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: 233.26  E-value: 1.72e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  69 QMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGKTLSF----IYDLKDQGGELLSLRYDLTVPFARYLAMNKI--- 141
Cdd:cd00773    1 EAALRRYIEDTLREVFERYGYEEIDTPVFEYTELFLRKSGDEvskeMYRFKDKGGRDLALRPDLTAPVARAVAENLLslp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 142 TNIKRYHIAKVYCRDNPAmtRGRYREFYQCDFDIAGqYDPMIPDAECLKIVHEILSDLELGDFRIKVNDKRILDGmfaVC 221
Cdd:cd00773   81 LPLKLYYIGPVFRYERPQ--KGRYREFYQVGVEIIG-SDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDG---IA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 222 GVPDDKFRTICSTVDKLDKmswedvksemvnekglseeaadqigqyvsmqggmdlaerllqdakmsqskqacAGLTDMKQ 301
Cdd:cd00773  155 GLLEDREEYIERLIDKLDK-----------------------------------------------------EALAHLEK 181

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 642099577 302 LFSYLQLFQVTDKVVFDLSLA----HYTGVIYEAILTQ 335
Cdd:cd00773  182 LLDYLEALGVDIKYSIDLSLVrgldYYTGIVFEAVADG 219
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
 56-334 2.84e-56

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 191.10  E-value: 2.84e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  56 LKTAKGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGK------TLSFIYDLKDQGGELLSLRYDLT 129
Cdd:PRK12420   4 MRNVKGTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKygggdeILKEIYTLTDQGKRDLALRYDLT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 130 VPFARYLAMNKitNI----KRYHIAKVYcRDNPaMTRGRYREFYQCDFDIAGQYDPMiPDAECLKIVHEILSDLELgDFR 205
Cdd:PRK12420  84 IPFAKVVAMNP--NIrlpfKRYEIGKVF-RDGP-IKQGRFREFIQCDVDIVGVESVM-AEAELMSMAFELFRRLNL-EVT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 206 IKVNDKRILDGMFAVCGVPDDKFRTICSTVDKLDKMSWEDVKSEmVNEKGLSEEAADQIGQYVSMQGGMDLAErlLQDAK 285
Cdd:PRK12420 158 IQYNNRKLLNGILQAIGIPTELTSDVILSLDKIEKIGIDGVRKD-LLERGISEEMADTICNTVLSCLQLSIAD--FKEAF 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 642099577 286 MSQSKQacAGLTDMKQLFSYLQLFQVTDKVVFDLSLAH----YTGVIYEAILT 334
Cdd:PRK12420 235 NNPLVA--EGVNELQQLQQYLIALGINENCIFNPFLARgltmYTGTVYEIFLK 285
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
 55-337 3.76e-56

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: 190.72  E-value: 3.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  55 TLKTAKGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGKT-------LsfIYDLKDQGGELLSLRYD 127
Cdd:COG0124    3 KIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIgedivekE--MYTFEDRGGRSLTLRPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 128 LTVPFARYLAMNKITN---IKRYHIAKVYCRDNPAmtRGRYREFYQCDFDIAGQYDPMIpDAECLKIVHEILSDLELGDF 204
Cdd:COG0124   81 GTAPVARAVAEHGNELpfpFKLYYIGPVFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEVIALAADLLKALGLKDF 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 205 RIKVNDkRildgmfavcGVPDDKFRTICSTVDKLDKMSWEDVksemvnekgLSEEAADQIGQYV----------SMQGGM 274
Cdd:COG0124  158 TLEINS-R---------GLPEERAEALLRYLDKLDKIGHEDV---------LDEDSQRRLETNPlraildskgpDCQEVL 218

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 642099577 275 DLAERLLQDAKMsqskqacAGLTDMKQLFSYLQLFQVtdKVVFDLSLAH----YTGVIYEAILTQNG 337
Cdd:COG0124  219 ADAPKLLDYLGE-------EGLAHFEEVLELLDALGI--PYVIDPRLVRgldyYTGTVFEIVTDGLG 276
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
 60-337 7.11e-52

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: 178.83  E-value: 7.11e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577   60 KGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGKT-------LSFIYDLKDQGGELLSLRYDLTVPF 132
Cdd:TIGR00442   4 RGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTELFKRKVgeetdivSKEMYTFKDKGGRSLTLRPEGTAPV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  133 ARYLAMNKITN---IKRYHIAKVYCRDNPAmtRGRYREFYQCDFDIAGQYDPMIpDAECLKIVHEILSDLELGDFRIKVN 209
Cdd:TIGR00442  84 ARAVIENKLLLpkpFKLYYIGPMFRYERPQ--KGRYRQFHQFGVEVIGSDSPLA-DAEIIALAADILKELGLKDFTLEIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  210 DKRILDGMFAvcgvpddKFRTICSTVDK-LDKMSWEDVKSEMVNEKGLSEEAADQIGQYVSmqggmdLAERLLQDAKMsq 288
Cdd:TIGR00442 161 SLGILEGRLE-------YREALIRYLDKhKDKLGEDSVRRLEKNPLRILDSKNEKIQELLK------NAPKILDFLCE-- 225

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 642099577  289 skqacAGLTDMKQLFSYLQLFQVtdKVVFDLSLA----HYTGVIYEAILTQNG 337
Cdd:TIGR00442 226 -----ESRAHFEELKELLDALGI--PYKIDPSLVrgldYYTGTVFEFVTDDLG 271
PLN02530 PLN02530
histidine-tRNA ligase
 49-331 6.25e-38

histidine-tRNA ligase


Pssm-ID: 178145 [Multi-domain]  Cd Length: 487  Bit Score: 143.34  E-value: 6.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  49 EGKHQFTLKTAKGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETLTGKTLSFI----YDLKDQGGELLSL 124
Cdd:PLN02530  63 DGKPKIDVNPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELYIRKAGEEItdqlYNFEDKGGRRVAL 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 125 RYDLTVPFARyLAMNKITNI----KRYHIAKvyCRDNPAMTRGRYREFYQCDFDIAGqYDPMIPDAECLKIVHEILSDLE 200
Cdd:PLN02530 143 RPELTPSLAR-LVLQKGKSLslplKWFAIGQ--CWRYERMTRGRRREHYQWNMDIIG-VPGVEAEAELLAAIVTFFKRVG 218

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 201 L--GDFRIKVNDKRILDGMFAVCGVPDDKFRTICSTVDKLDKMSWEDVKSEMvNEKGLSEEAADQIGQYVSMQGGMDLAE 278
Cdd:PLN02530 219 ItsSDVGIKVSSRKVLQAVLKSYGIPEESFAPVCVIVDKLEKLPREEIEKEL-DTLGVSEEAIEGILDVLSLKSLDDLEA 297

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 642099577 279 RLLQDAKmsqskqacaGLTDMKQLFSYLQLFQVTDKVVFDLS----LAHYTGVIYEA 331
Cdd:PLN02530 298 LLGADSE---------AVADLKQLFSLAEAYGYQDWLVFDASvvrgLAYYTGIVFEG 345
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
 61-331 8.18e-27

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: 109.21  E-value: 8.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577   61 GTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFELKETL---TGKTLSFIYDLKDQGGELLSLRYDLTVPFARYLA 137
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLltgTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  138 mnkiTNIKRYHIAKV-YC----RDNPAMTRGRyREFYQCDFDIAGQYDPMiPDAECLKIVHEILSDLELGDFRIKVNDKR 212
Cdd:pfam13393  81 ----HRLNRPGPLRLcYAgsvlRTRPKGLGRS-REPLQVGAELIGHAGIE-ADAEIISLLLEALAAAGVPGVTLDLGHVG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  213 ILDGMFAVCGVPDDKFRTICSTVDKLDkmsWEDVKsEMVNEKGLSEEAADQIGQYVSMQGGMDLAERLLQDakMSQSKQA 292
Cdd:pfam13393 155 LVRALLEAAGLSEALEEALRAALQRKD---AAELA-ELAAEAGLPPALRRALLALPDLYGGPEVLDEARAA--LPGLPAL 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 642099577  293 CAGLTDMKQLFSYLQLFQVTDKVVFDLSLAH----YTGVIYEA 331
Cdd:pfam13393 229 QEALDELEALAALLEALGDGVRLTFDLAELRgyeyYTGIVFAA 271
HisRS_RNA cd00938
HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS ...
 5-49 3.05e-19

HisRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of HisRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238474 [Multi-domain]  Cd Length: 45  Bit Score: 80.59  E-value: 3.05e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 642099577   5 AQIQDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQIGGDE 49
Cdd:cd00938    1 AKLEEAVKLQGELVRKLKAEKASKEQIAEEVAKLLELKAQLGGDE 45
WHEP-TRS pfam00458
WHEP-TRS domain;
7-69 1.96e-15

WHEP-TRS domain;


Pssm-ID: 459819 [Multi-domain]  Cd Length: 53  Bit Score: 69.83  E-value: 1.96e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 642099577    7 IQDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQiggdegkhqftLKTAKGTrDYNPKQ 69
Cdd:pfam00458   1 LTEKIKAQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQ-----------YKALTGK-DYKPGA 51
WHEPGMRS_RNA cd01200
EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher ...
 8-49 3.44e-14

EPRS-like_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in three copies in the mammalian bifunctional EPRS in a region that separates the N-terminal GluRS from the C-terminal ProRS. In the Drosophila EPRS, this domain is repeated six times. It is found at the N-terminus of TrpRS, HisRS and GlyR and at the C-terminus of MetRS. This domain consists of a helix- turn- helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238605 [Multi-domain]  Cd Length: 42  Bit Score: 66.02  E-value: 3.44e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 642099577   8 QDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQIGGDE 49
Cdd:cd01200    1 YEKIAEQGDLVRKLKAEKAPKEEIDAAVKKLLALKAQYKEAT 42
WHEP-TRS smart00991
A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of ...
 8-51 8.45e-14

A conserved domain of 46 amino acids, called WHEP-TRS has been shown.to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases; This domain is present one to six times in the several enzymes. There are three copies in mammalian multifunctional aminoacyl-tRNA synthetase in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain, and six copies in the intercatalytic region of the Drosophila enzyme. The domain is found at the N-terminal extremity of the mammalian tryptophanyl- tRNA synthetase and histidyl-tRNA synthetase, and the mammalian, insect, nematode and plant glycyl- tRNA synthetases. This domain could contain a central alpha-helical region and may play a role in the association of tRNA-synthetases into multienzyme complexes.


Pssm-ID: 214960 [Multi-domain]  Cd Length: 56  Bit Score: 65.44  E-value: 8.45e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 642099577     8 QDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQIGGDEGK 51
Cdd:smart00991   1 EEAVAAQGELVRKLKAEKASKDEIDAAVAKLLALKAQLKEATGQ 44
WEPRS_RNA cd00936
WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote ...
 11-44 3.39e-11

WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates the N-terminal glutamyl-tRNA synthetase (GluRS) from the C-terminal prolyl-tRNA synthetase (ProRS). It is also found at the N-terminus of vertebrate tryptophanyl-tRNA synthetases (TrpRS). This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238473 [Multi-domain]  Cd Length: 50  Bit Score: 58.02  E-value: 3.39e-11
                         10        20        30
                 ....*....|....*....|....*....|....
gi 642099577  11 IKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQ 44
Cdd:cd00936    5 IAAQGDLVRELKAKKAPKEEIDAAVKKLLALKAD 38
hisZ PRK12295
ATP phosphoribosyltransferase regulatory subunit; Provisional
 70-225 4.49e-11

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183413 [Multi-domain]  Cd Length: 373  Bit Score: 63.80  E-value: 4.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  70 MAIRERVFNTIIRCFKHHGAETIDTPVFELKET---LTGKTL-SFIYDLKDQGGELLSLRYDLTVPFAR-YLAMNKITNI 144
Cdd:PRK12295   4 LSASAAAAEALLASFEAAGAVRVDPPILQPAEPfldLSGEDIrRRIFVTSDENGEELCLRPDFTIPVCRrHIATAGGEPA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 145 KRYHIAKVYcRdnpaMTRGRYREFYQCDFDIAGQYDPMIPDAECLKIVHEILSDLELGDFRIKVNDKRILDGMFAVCGVP 224
Cdd:PRK12295  84 RYAYLGEVF-R----QRRDRASEFLQAGIESFGRADPAAADAEVLALALEALAALGPGDLEVRLGDVGLFAALVDALGLP 158


                 .
gi 642099577 225 D 225
Cdd:PRK12295 159 P 159
syh CHL00201
histidine-tRNA synthetase; Provisional
 60-209 4.96e-09

histidine-tRNA synthetase; Provisional


Pssm-ID: 164576 [Multi-domain]  Cd Length: 430  Bit Score: 57.99  E-value: 4.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  60 KGTRDYNPKQMAIRERVFNTIIRCFKHHGAETIDTPVFE---LKETLTGKTLSFI----YDLKDQGGELLSLRYDLTVPF 132
Cdd:CHL00201   8 RGTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFEnssLYDRGIGETTDIVnkemYRFTDRSNRDITLRPEGTAGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 133 ARYLAMNKIT---NIKR-YHIAKVYCRDNPamTRGRYREFYQCDFDIAGQYDPMiPDAECLKIVHEILSDLELGDFRIKV 208
Cdd:CHL00201  88 VRAFIENKMDyhsNLQRlWYSGPMFRYERP--QSGRQRQFHQLGIEFIGSIDAR-ADTEVIHLAMQIFNELQVKNLILDI 164


                 .
gi 642099577 209 N 209
Cdd:CHL00201 165 N 165
MetRS_RNA cd00939
MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in ...
 7-51 5.01e-08

MetRS_RNA binding domain. This short RNA-binding domain is found at the C-terminus of MetRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is repeated in Drosophila MetRS. This domain consists of a helix-turn-helix structure, which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238475 [Multi-domain]  Cd Length: 45  Bit Score: 49.01  E-value: 5.01e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 642099577   7 IQDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQIGGDEGK 51
Cdd:cd00939    1 LEKEVAEQGNKVRKLKASKADKSVWQPEVNKLLDLKKQLALAEGK 45
PLN02734 PLN02734
glycyl-tRNA synthetase
 5-88 9.87e-06

glycyl-tRNA synthetase


Pssm-ID: 178335 [Multi-domain]  Cd Length: 684  Bit Score: 47.82  E-value: 9.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577   5 AQIQDAIKTQGEVVRKLKTEKASKEQIDEEVAKLLKLKAQIGGDEgKHQFTLKTAKGTRDYNPKqmAIRERVFNTIIR-- 82
Cdd:PLN02734  10 AEKQAAVTAQGNAVRALKASKADKAEIDAAIEKLKALKLEKSALE-KELQAAVGAGGDGAASKE--AFRQAVVNTLERrl 86

                         90
                 ....*....|
gi 642099577  83 ----CFKHHG 88
Cdd:PLN02734  87 fyipSFKIYG 96
GlyRS_RNA cd00935
GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS ...
 5-38 3.45e-04

GlyRS_RNA binding domain. This short RNA-binding domain is found at the N-terminus of GlyRS in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). This domain consists of a helix-turn-helix structure , which is similar to other RNA-binding proteins. It is involved in both protein-RNA interactions by binding tRNA and protein-protein interactions, which are important for the formation of aaRSs into multienzyme complexes.


Pssm-ID: 238472 [Multi-domain]  Cd Length: 51  Bit Score: 38.24  E-value: 3.45e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 642099577   5 AQIQDAIKTQGEVVRKLKTEKASKEQIDEEVAKL 38
Cdd:cd00935    2 APLRAAVKEQGDLVRKLKEEGAPDVDIKKAVAEL 35
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
 72-233 3.81e-03

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: 38.64  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577  72 IRERVFNTIIRCFKHHGAETIDTPVFELKETLTGKTLSFIYDL--KDQGGELLSLRYDLTvPFARYLAMNKITNI--KRY 147
Cdd:cd00768    1 IRSKIEQKLRRFMAELGFQEVETPIVEREPLLEKAGHEPKDLLpvGAENEEDLYLRPTLE-PGLVRLFVSHIRKLplRLA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 642099577 148 HIAKVYCRDNPAMTRGRYREFYQCDFDIAGQYDPMIP-DAECLKIVHEILSDLELGD---FRIKVNDKrILDGMFAVCG- 222
Cdd:cd00768   80 EIGPAFRNEGGRRGLRRVREFTQLEGEVFGEDGEEASeFEELIELTEELLRALGIKLdivFVEKTPGE-FSPGGAGPGFe 158

                        170
                 ....*....|....*
gi 642099577 223 ----VPDDKFRTICS 233
Cdd:cd00768  159 ievdHPEGRGLEIGS 173
 
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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