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Conserved domains on  [gi|502824746|ref|WP_013059722|]
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MULTISPECIES: ATP phosphoribosyltransferase regulatory subunit [Priestia]

Protein Classification

ATP phosphoribosyltransferase regulatory subunit( domain architecture ID 11485747)

ATP phosphoribosyltransferase regulatory subunit is required for the first step of histidine biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
5-381 7.35e-157

ATP phosphoribosyltransferase regulatory subunit; Provisional


:

Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 447.01  E-value: 7.35e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   5 FMFEKPLGMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASA-ILDQQLFKLLDK-EGHTLVLRPDV 82
Cdd:PRK12292   1 MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGaILDLRTFKLVDQlSGRTLGLRPDM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  83 TTPFARVAASKLLNNS-PLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAI 161
Cdd:PRK12292  81 TAQIARIAATRLANRPgPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 162 GHIGFVNSLFLEIVGNEERANVLRRFLYEKNYVGYRNHVKdlNLSSIDKQRLLQLLNLRGDEKKIEEAVELVENEAGKKA 241
Cdd:PRK12292 161 GHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEELVL--DLSEELRDALLALPRLRGGREVLEEARKLLPSLPIKRA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 242 AGDLKKLWNMLDAYGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRLIE 321
Cdd:PRK12292 239 LDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGNPIASGGRYDDLLGRFGRARPATGFSLDLDRLLE 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502824746 322 ALGEEVYEPSAVYGILYSQERLDEALALAAEQRKQGYRVVTQEIA-GVDDVDVFTAQFEEV 381
Cdd:PRK12292 319 LQLELPVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVLALPGrNFEDAREYARDRQIV 379
 
Name Accession Description Interval E-value
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
5-381 7.35e-157

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 447.01  E-value: 7.35e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   5 FMFEKPLGMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASA-ILDQQLFKLLDK-EGHTLVLRPDV 82
Cdd:PRK12292   1 MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGaILDLRTFKLVDQlSGRTLGLRPDM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  83 TTPFARVAASKLLNNS-PLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAI 161
Cdd:PRK12292  81 TAQIARIAATRLANRPgPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 162 GHIGFVNSLFLEIVGNEERANVLRRFLYEKNYVGYRNHVKdlNLSSIDKQRLLQLLNLRGDEKKIEEAVELVENEAGKKA 241
Cdd:PRK12292 161 GHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEELVL--DLSEELRDALLALPRLRGGREVLEEARKLLPSLPIKRA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 242 AGDLKKLWNMLDAYGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRLIE 321
Cdd:PRK12292 239 LDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGNPIASGGRYDDLLGRFGRARPATGFSLDLDRLLE 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502824746 322 ALGEEVYEPSAVYGILYSQERLDEALALAAEQRKQGYRVVTQEIA-GVDDVDVFTAQFEEV 381
Cdd:PRK12292 319 LQLELPVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVLALPGrNFEDAREYARDRQIV 379
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
17-326 6.92e-116

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


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 339.85  E-value: 6.92e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  17 LPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETV-GSASAILDQQLFKLLDKEGHTLVLRPDVTTPFARVAASKLL 95
Cdd:COG3705    1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLlTGSGADLDLQTFKLVDQLGRTLGLRPDMTPQVARIAATRLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  96 NNS-PLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGHIGFVNSLFLEI 174
Cdd:COG3705   81 NRPgPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 175 VGNEERANVLRRFLYEKNYVGYRNHVKDLNLSSIDKQRLLQLLNLRGDEKKIEEAVELVENEAGKKAAGDLKKLWNMLDA 254
Cdd:COG3705  161 GLSEEQREELRRALARKDAVELEELLAELGLSEELAEALLALPELYGGEEVLARARALLLDAAIRAALDELEALAEALAA 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502824746 255 YGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRLIEALGEE 326
Cdd:COG3705  241 RGPDVRLTFDLSELRGYDYYTGIVFEAYAPGVGDPLARGGRYDGLLAAFGRARPATGFSLDLDRLLRALPAA 312
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
14-324 6.50e-109

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: 322.26  E-value: 6.50e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   14 RDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASAILDQQLFKLLDKEGHTLVLRPDVTTPFARVAASK 93
Cdd:TIGR00443   1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLVSTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   94 LLNNS-PLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGHIGFVNSLFL 172
Cdd:TIGR00443  81 LRDRPlPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  173 EIVGNEERANVLRRFLYEKNYVGYRNHVKDLNLSSIDKQRLLQLLNLRGD-EKKIEEAVELVENEAGKKAAGDLKKLWNM 251
Cdd:TIGR00443 161 EAGLPEEAREALREALARKDLVALEELVAELGLSPEVRERLLALPRLRGDgEEVLEEARALAGSETAEAALDELEAVLEL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502824746  252 LDAYGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRLIEALG 324
Cdd:TIGR00443 241 LEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAPLAGGGRYDELLGRFGRPLPATGFALNLERLLEALT 313
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
12-319 8.02e-75

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: 234.79  E-value: 8.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   12 GMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASAILDQQLFKLLDKEGHTLVLRPDVTTPFARVAA 91
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   92 SKLLNNSPLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGHIGFVNSLF 171
Cdd:pfam13393  81 HRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  172 LEIVGNEERANVLRRFLYEKNYVGYRNHVKDLNLSSIDKQRLLQLLNLRGDEKKIEEAVE-LVENEAGKKAAGDLKKLWN 250
Cdd:pfam13393 161 EAAGLSEALEEALRAALQRKDAAELAELAAEAGLPPALRRALLALPDLYGGPEVLDEARAaLPGLPALQEALDELEALAA 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502824746  251 MLDAYGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRL 319
Cdd:pfam13393 241 LLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVGEPLARGGRYDDLGAAFGRARPATGFSLDLEAL 309
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
22-323 1.79e-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: 232.11  E-value: 1.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  22 ERKKQVRNQLADEIGSWGYQYMATPTVEYYET-VGSASAILDQQLFKLLDKEGHTLVLRPDVTTPFARVAASKLLN-NSP 99
Cdd:cd00773    3 ALRRYIEDTLREVFERYGYEEIDTPVFEYTELfLRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSlPLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 100 LRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGHIGFVNSLFLeivgnee 179
Cdd:cd00773   83 LKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAG------- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 180 ranvlrrflyeknyvgyrnhvkDLNLssidkqrllqllnlrgDEKKIEEAVELVENEAGKkaagDLKKLWNMLDAYGVTD 259
Cdd:cd00773  156 ----------------------LLED----------------REEYIERLIDKLDKEALA----HLEKLLDYLEALGVDI 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502824746 260 EIKIDFNLVSHMSYYTGILFEVFAEN--VGFHIGNGGRYDQLLE-KFASKTPATGFGIQLDRLIEAL 323
Cdd:cd00773  194 KYSIDLSLVRGLDYYTGIVFEAVADGlgAQGSIAGGGRYDGLLEeFGGEDVPAVGFAIGLERLLLAL 260
 
Name Accession Description Interval E-value
hisZ PRK12292
ATP phosphoribosyltransferase regulatory subunit; Provisional
5-381 7.35e-157

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237043 [Multi-domain]  Cd Length: 391  Bit Score: 447.01  E-value: 7.35e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   5 FMFEKPLGMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASA-ILDQQLFKLLDK-EGHTLVLRPDV 82
Cdd:PRK12292   1 MMWQLPEGIRDLLPEEARKIEEIRRRLLDLFRRWGYEEVITPTLEYLDTLLAGGGaILDLRTFKLVDQlSGRTLGLRPDM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  83 TTPFARVAASKLLNNS-PLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAI 161
Cdd:PRK12292  81 TAQIARIAATRLANRPgPLRLCYAGNVFRAQERGLGRSREFLQSGVELIGDAGLEADAEVILLLLEALKALGLPNFTLDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 162 GHIGFVNSLFLEIVGNEERANVLRRFLYEKNYVGYRNHVKdlNLSSIDKQRLLQLLNLRGDEKKIEEAVELVENEAGKKA 241
Cdd:PRK12292 161 GHVGLFRALLEAAGLSEELEEVLRRALANKDYVALEELVL--DLSEELRDALLALPRLRGGREVLEEARKLLPSLPIKRA 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 242 AGDLKKLWNMLDAYGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRLIE 321
Cdd:PRK12292 239 LDELEALAEALEKYGYGIPLSLDLGLLRHLDYYTGIVFEGYVDGVGNPIASGGRYDDLLGRFGRARPATGFSLDLDRLLE 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502824746 322 ALGEEVYEPSAVYGILYSQERLDEALALAAEQRKQGYRVVTQEIA-GVDDVDVFTAQFEEV 381
Cdd:PRK12292 319 LQLELPVEARKDLVIAPDSEALAAALAAAQELRKKGEIVVLALPGrNFEDAREYARDRQIV 379
HisZ COG3705
ATP phosphoribosyltransferase regulatory subunit HisZ [Amino acid transport and metabolism];
17-326 6.92e-116

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


Pssm-ID: 442919 [Multi-domain]  Cd Length: 312  Bit Score: 339.85  E-value: 6.92e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  17 LPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETV-GSASAILDQQLFKLLDKEGHTLVLRPDVTTPFARVAASKLL 95
Cdd:COG3705    1 LPEEAARKEELRRRLLDVFRSWGYELVEPPLLEYLDSLlTGSGADLDLQTFKLVDQLGRTLGLRPDMTPQVARIAATRLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  96 NNS-PLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGHIGFVNSLFLEI 174
Cdd:COG3705   81 NRPgPLRLCYAGNVFRTRPSGLGRSREFLQAGAELIGHAGLEADAEVIALALEALKAAGLEDFTLDLGHVGLFRALLEAL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 175 VGNEERANVLRRFLYEKNYVGYRNHVKDLNLSSIDKQRLLQLLNLRGDEKKIEEAVELVENEAGKKAAGDLKKLWNMLDA 254
Cdd:COG3705  161 GLSEEQREELRRALARKDAVELEELLAELGLSEELAEALLALPELYGGEEVLARARALLLDAAIRAALDELEALAEALAA 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502824746 255 YGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRLIEALGEE 326
Cdd:COG3705  241 RGPDVRLTFDLSELRGYDYYTGIVFEAYAPGVGDPLARGGRYDGLLAAFGRARPATGFSLDLDRLLRALPAA 312
hisZ_biosyn_reg TIGR00443
ATP phosphoribosyltransferase, regulatory subunit; Apparant second copies of histidyl-tRNA ...
14-324 6.50e-109

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: 322.26  E-value: 6.50e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   14 RDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASAILDQQLFKLLDKEGHTLVLRPDVTTPFARVAASK 93
Cdd:TIGR00443   1 RDLLPEEAARKEEIERQLQDVFRSWGYQEIITPTLEYLDTLSAGSGILNEDLFKLFDQLGRVLGLRPDMTAPIARLVSTR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   94 LLNNS-PLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGHIGFVNSLFL 172
Cdd:TIGR00443  81 LRDRPlPLRLCYAGNVFRTNESGGGRSREFTQAGVELIGAGGPAADAEVIALLIEALKALGLKDFKIELGHVGLVRALLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  173 EIVGNEERANVLRRFLYEKNYVGYRNHVKDLNLSSIDKQRLLQLLNLRGD-EKKIEEAVELVENEAGKKAAGDLKKLWNM 251
Cdd:TIGR00443 161 EAGLPEEAREALREALARKDLVALEELVAELGLSPEVRERLLALPRLRGDgEEVLEEARALAGSETAEAALDELEAVLEL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502824746  252 LDAYGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRLIEALG 324
Cdd:TIGR00443 241 LEARGVEEYISLDLGLVRGYHYYTGLIFEGYAPGLGAPLAGGGRYDELLGRFGRPLPATGFALNLERLLEALT 313
tRNA-synt_His pfam13393
Histidyl-tRNA synthetase; This is a family of class II aminoacyl-tRNA synthetase-like and ATP ...
12-319 8.02e-75

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: 234.79  E-value: 8.02e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   12 GMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASAILDQQLFKLLDKEGHTLVLRPDVTTPFARVAA 91
Cdd:pfam13393   1 GIRDLLPPEARRIEELRRRLLDLFRSWGYELVMPPLLEYLDSLLTGTGADLDQTFKLVDQSGRLLGLRADITPQVARIDA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   92 SKLLNNSPLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGHIGFVNSLF 171
Cdd:pfam13393  81 HRLNRPGPLRLCYAGSVLRTRPKGLGRSREPLQVGAELIGHAGIEADAEIISLLLEALAAAGVPGVTLDLGHVGLVRALL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  172 LEIVGNEERANVLRRFLYEKNYVGYRNHVKDLNLSSIDKQRLLQLLNLRGDEKKIEEAVE-LVENEAGKKAAGDLKKLWN 250
Cdd:pfam13393 161 EAAGLSEALEEALRAALQRKDAAELAELAAEAGLPPALRRALLALPDLYGGPEVLDEARAaLPGLPALQEALDELEALAA 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502824746  251 MLDAYGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRL 319
Cdd:pfam13393 241 LLEALGDGVRLTFDLAELRGYEYYTGIVFAAYAPGVGEPLARGGRYDDLGAAFGRARPATGFSLDLEAL 309
HisRS-like_core cd00773
Class II Histidinyl-tRNA synthetase (HisRS)-like catalytic core domain. HisRS is a homodimer. ...
22-323 1.79e-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: 232.11  E-value: 1.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  22 ERKKQVRNQLADEIGSWGYQYMATPTVEYYET-VGSASAILDQQLFKLLDKEGHTLVLRPDVTTPFARVAASKLLN-NSP 99
Cdd:cd00773    3 ALRRYIEDTLREVFERYGYEEIDTPVFEYTELfLRKSGDEVSKEMYRFKDKGGRDLALRPDLTAPVARAVAENLLSlPLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 100 LRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGHIGFVNSLFLeivgnee 179
Cdd:cd00773   83 LKLYYIGPVFRYERPQKGRYREFYQVGVEIIGSDSPLADAEVIALAVEILEALGLKDFQIKINHRGILDGIAG------- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 180 ranvlrrflyeknyvgyrnhvkDLNLssidkqrllqllnlrgDEKKIEEAVELVENEAGKkaagDLKKLWNMLDAYGVTD 259
Cdd:cd00773  156 ----------------------LLED----------------REEYIERLIDKLDKEALA----HLEKLLDYLEALGVDI 193
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502824746 260 EIKIDFNLVSHMSYYTGILFEVFAEN--VGFHIGNGGRYDQLLE-KFASKTPATGFGIQLDRLIEAL 323
Cdd:cd00773  194 KYSIDLSLVRGLDYYTGIVFEAVADGlgAQGSIAGGGRYDGLLEeFGGEDVPAVGFAIGLERLLLAL 260
HisS COG0124
Histidyl-tRNA synthetase [Translation, ribosomal structure and biogenesis]; Histidyl-tRNA ...
6-362 4.44e-70

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: 226.16  E-value: 4.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   6 MFEKPLGMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASA--ILDQQLFKLLDKEGHTLVLRPDVT 83
Cdd:COG0124    3 KIQAPRGTRDILPEESAKWQYVEDTIREVFERYGFQEIRTPIFEYTELFARKIGedIVEKEMYTFEDRGGRSLTLRPEGT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  84 TPFARVAASKLLNNS-PLRLAYEANVFRA--QQRegGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVA 160
Cdd:COG0124   83 APVARAVAEHGNELPfPFKLYYIGPVFRYerPQK--GRYRQFHQFGVEVIGSDSPLADAEVIALAADLLKALGLKDFTLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 161 IGHIGFvnslfleivgNEERANVLRRFLYEKNYVGyrnHVKDLNLSSIDKQRLLQLLN-----LRGDEKKIEEAVELVEN 235
Cdd:COG0124  161 INSRGL----------PEERAEALLRYLDKLDKIG---HEDVLDEDSQRRLETNPLRAildskGPDCQEVLADAPKLLDY 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 236 EaGKKAAGDLKKLWNMLDAYGVtdEIKIDFNLVSHMSYYTGILFEVFAENVGFH--IGNGGRYDQLLEKFASK-TPATGF 312
Cdd:COG0124  228 L-GEEGLAHFEEVLELLDALGI--PYVIDPRLVRGLDYYTGTVFEIVTDGLGAQgsVCGGGRYDGLVEQLGGPpTPAVGF 304
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502824746 313 GIQLDRLIEALGEEVYEPSA-----VYGILYSQERLDEALALAAEQRKQGYRVVT 362
Cdd:COG0124  305 AIGLERLLLLLEELGLLPAAepppdVYVVPLGEEARAEALKLAQELRAAGIRVEL 359
hisS TIGR00442
histidyl-tRNA synthetase; This model finds a histidyl-tRNA synthetase in every completed ...
8-362 1.66e-64

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: 211.18  E-value: 1.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746    8 EKPLGMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYE----TVGSASAILDQQLFKLLDKEGHTLVLRPDVT 83
Cdd:TIGR00442   1 QKPRGTRDFLPEEMIKWQYIEETIREVFERYGFKEIRTPIFEYTElfkrKVGEETDIVSKEMYTFKDKGGRSLTLRPEGT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   84 TPFAR-VAASKLLNNSPLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIG 162
Cdd:TIGR00442  81 APVARaVIENKLLLPKPFKLYYIGPMFRYERPQKGRYRQFHQFGVEVIGSDSPLADAEIIALAADILKELGLKDFTLEIN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  163 HIGFVNSLFleivgneERANVLRRFLyEKNyvgyrnhvKDlNLSSIDKQRLLQLLNLRGDEKK------IEEAVELVENe 236
Cdd:TIGR00442 161 SLGILEGRL-------EYREALIRYL-DKH--------KD-KLGEDSVRRLEKNPLRILDSKNekiqelLKNAPKILDF- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  237 AGKKAAGDLKKLWNMLDAYGVtdEIKIDFNLVSHMSYYTGILFEVFAENVGFH--IGNGGRYDQLLEKFA-SKTPATGFG 313
Cdd:TIGR00442 223 LCEESRAHFEELKELLDALGI--PYKIDPSLVRGLDYYTGTVFEFVTDDLGAQgsICGGGRYDGLVEELGgPPTPAVGFA 300
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 502824746  314 IQLDRLIEALGEEVYEPSA-----VYGILYSQERLDEALALAAEQRKQGYRVVT 362
Cdd:TIGR00442 301 IGIERLILLLEELGLIPPPskkpdVYVVPLGEEAELEALKLAQKLRKAGIRVEV 354
PRK12421 PRK12421
ATP phosphoribosyltransferase regulatory subunit; Provisional
10-363 7.16e-40

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 237098  Cd Length: 392  Bit Score: 145.88  E-value: 7.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  10 PLGMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETV-GSASAILDQQLFKLLDK-EGHTLVLRPDVTTPFA 87
Cdd:PRK12421  10 PDGVADVLPEEAQKIERLRRRLLDLFASRGYQLVMPPLIEYLESLlTGAGQDLKLQTFKLIDQlSGRLMGVRADITPQVA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  88 RVAASKLLNNSPLRLAYEANVFRAqqreggRPAEFE------QIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAI 161
Cdd:PRK12421  90 RIDAHLLNREGVARLCYAGSVLHT------LPQGLFgsrtplQLGAELYGHAGIEADLEIIRLMLGLLRNAGVPALHLDL 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 162 GHIGFVNSLFLEIVGNEERANVLRRFLYEKNYVGYRNHVKDLNLSSIDKQRLLQLLNLRGDEKKIEEA-VELVENEAG-K 239
Cdd:PRK12421 164 GHVGIFRRLAELAGLSPEEEEELFDLLQRKALPELAEVCQNLGVGSDLRRMFYALARLNGGLEALDRAlSVLALQDAAiR 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 240 KAAGDLKKLWNMLDAYGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGFHIGNGGRYDQLLEKFASKTPATGFGIQLDRL 319
Cdd:PRK12421 244 QALDELKTLAAHLKNRWPELPVSIDLAELRGYHYHTGLVFAAYIPGRGQALARGGRYDGIGEAFGRARPATGFSMDLKEL 323
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 502824746 320 IeALGEEVYEPSAVYGILYSQERLDEALALAaeqRKQGYRVVTQ 363
Cdd:PRK12421 324 L-ALQFLEEEAGAILAPWGDDPDLLAAIAEL---RQQGERVVQL 363
PRK12420 PRK12420
histidyl-tRNA synthetase; Provisional
12-360 4.83e-24

histidyl-tRNA synthetase; Provisional


Pssm-ID: 237097 [Multi-domain]  Cd Length: 423  Bit Score: 102.89  E-value: 4.83e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  12 GMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASA----ILdQQLFKLLDKEGHTLVLRPDVTTPFA 87
Cdd:PRK12420   9 GTKDYLPEEQVLRNKIKRALEDVFERYGCKPLETPTLNMYELMSSKYGggdeIL-KEIYTLTDQGKRDLALRYDLTIPFA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  88 RVAASkllnNSPLRLA---YE-ANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLkSFKVAIGH 163
Cdd:PRK12420  88 KVVAM----NPNIRLPfkrYEiGKVFRDGPIKQGRFREFIQCDVDIVGVESVMAEAELMSMAFELFRRLNL-EVTIQYNN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 164 IGFVNSLFLEIVGNEERAN--VLRRFLYEKNYV-GYRNHVKDLNLSSiDKQRLLQLLNLRGDEKKIEEAVELVENEAGKK 240
Cdd:PRK12420 163 RKLLNGILQAIGIPTELTSdvILSLDKIEKIGIdGVRKDLLERGISE-EMADTICNTVLSCLQLSIADFKEAFNNPLVAE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 241 AAGDLKKLWNMLDAYGVTDEIKIDFNLVSHMSYYTGILFEVFAENVGF--HIGNGGRYDQLLEKFASKT---PATGFGIQ 315
Cdd:PRK12420 242 GVNELQQLQQYLIALGINENCIFNPFLARGLTMYTGTVYEIFLKDGSItsSIGSGGRYDNIIGAFRGDDmnyPTVGISFG 321
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 502824746 316 LDRLIEALG-EEVYEPSAVYGILYSQERLdEALALAAEQRK-QGYRV 360
Cdd:PRK12420 322 LDVIYTALSqKETISSTADVFIIPLGTEL-QCLQIAQQLRStTGLKV 367
syh CHL00201
histidine-tRNA synthetase; Provisional
12-320 2.44e-21

histidine-tRNA synthetase; Provisional


Pssm-ID: 164576 [Multi-domain]  Cd Length: 430  Bit Score: 94.97  E-value: 2.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  12 GMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVE----YYETVGSASAILDQQLFKLLDKEGHTLVLRPDVTTPFA 87
Cdd:CHL00201   9 GTKDILPDEINYWQFIHDKALTLLSLANYSEIRTPIFEnsslYDRGIGETTDIVNKEMYRFTDRSNRDITLRPEGTAGIV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  88 RVAASKLLN--NSPLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGHIG 165
Cdd:CHL00201  89 RAFIENKMDyhSNLQRLWYSGPMFRYERPQSGRQRQFHQLGIEFIGSIDARADTEVIHLAMQIFNELQVKNLILDINSIG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 166 FVnslfleivgnEERANvlrrflYEKNYVGY-RNHVKDLNLSSIDKQRLLQLLNLRGDEKKIEEavelVENEAGKkaagd 244
Cdd:CHL00201 169 KL----------EDRQS------YQLKLVEYlSQYQDDLDTDSQNRLYSNPIRILDSKNLKTQE----ILDGAPK----- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 245 LKKLWNMLDA---YGVTDEI-------KIDFNLVSHMSYYTGILFEV--FAENVGFHIGNGGRYDQLLEKF-ASKTPATG 311
Cdd:CHL00201 224 ISDFLSLESTehfYDVCTYLnllnipyKINYKLVRGLDYYNDTAFEIktLSSNGQDTICGGGRYDSLIHQLgGPKTPAVG 303

                 ....*....
gi 502824746 312 FGIQLDRLI 320
Cdd:CHL00201 304 CAIGLERLL 312
PLN02972 PLN02972
Histidyl-tRNA synthetase
45-352 3.03e-21

Histidyl-tRNA synthetase


Pssm-ID: 215525 [Multi-domain]  Cd Length: 763  Bit Score: 95.72  E-value: 3.03e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  45 TPTVEYYETVGSASAILDQQLFKLLDKEGHTLVLRPDVTTPFARVAAsklLNN-SPLRLAYEANVFRAQQREGGRPAEFE 123
Cdd:PLN02972 365 TPVFELRETLMGKYGEDSKLIYDLADQGGELCSLRYDLTVPFARYVA---MNGiTSFKRYQIAKVYRRDNPSKGRYREFY 441
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 124 QIGVELIGD-ATMSSDAEVIALMIGALKRAGLKSFKVAIGHIGFVNSLfLEIVG-----------------NEERANVLR 185
Cdd:PLN02972 442 QCDFDIAGVyEPMGPDFEIIKVLTELLDELDIGTYEVKLNHRKLLDGM-LEICGvppekfrticssidkldKQSFEQVKK 520
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 186 RFLYEKnyvGYRNHVKDlnlsSIDKQRLLQLLNLRGDEKKIEEAVELVENEAGKKAAGDLKKLWNMLDAYGVTDEIKIDF 265
Cdd:PLN02972 521 EMVEEK---GLSNETAD----KIGNFVKERGPPLELLSKLRQEGSEFLGNASSRAALDELEIMFKALEKSKAIGKIVFDL 593
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 266 NLVSHMSYYTGILFE-VF-AENVGfHIGNGGRYDQLLEKFASK-TPATGFGIQLDRLIEALGEEVYEPSAVYGILYSQER 342
Cdd:PLN02972 594 SLARGLDYYTGVIYEaVFkGAQVG-SIAAGGRYDNLVGMFSGKqVPAVGVSLGIERVFAIMEQQEEEKSQVIRPTETEVL 672
                        330
                 ....*....|....
gi 502824746 343 L----DEALALAAE 352
Cdd:PLN02972 673 VsiigDDKLALAAE 686
PLN02530 PLN02530
histidine-tRNA ligase
8-360 1.44e-19

histidine-tRNA ligase


Pssm-ID: 178145 [Multi-domain]  Cd Length: 487  Bit Score: 90.19  E-value: 1.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746   8 EKPLGMRDTLPALFERKKQVRNQLADEIGSWGYQYMATPTVEYYET-VGSASAILDQQLFKLLDKEGHTLVLRPDVTTPF 86
Cdd:PLN02530  71 NPPKGTRDFPPEDMRLRNWLFDHFREVSRLFGFEEVDAPVLESEELyIRKAGEEITDQLYNFEDKGGRRVALRPELTPSL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  87 ARVAASKLLNNS-PLRLAYEANVFRAQQREGGRPAEFEQIGVELIGDATMSSDAEVIALMIGALKRAGLKSFKVAIGhig 165
Cdd:PLN02530 151 ARLVLQKGKSLSlPLKWFAIGQCWRYERMTRGRRREHYQWNMDIIGVPGVEAEAELLAAIVTFFKRVGITSSDVGIK--- 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 166 fVNSlfleivgNEERANVLRRFLYEKNYVGYRNHVKDlNLSSIDKQRLLQLLNLRG-DEKKIEEAVELVENE-------- 236
Cdd:PLN02530 228 -VSS-------RKVLQAVLKSYGIPEESFAPVCVIVD-KLEKLPREEIEKELDTLGvSEEAIEGILDVLSLKslddleal 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 237 --AGKKAAGDLKKLWNMLDAYGVTDEIKIDFNLVSHMSYYTGILFEVF-AENVGFHIGNGGRYDQLLEKFASK-TPATGF 312
Cdd:PLN02530 299 lgADSEAVADLKQLFSLAEAYGYQDWLVFDASVVRGLAYYTGIVFEGFdRAGKLRAICGGGRYDRLLSTFGGEdTPACGF 378
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502824746 313 GIQLDRLIEALGEEVYEPSAVYGILYSQERLDEAL-----ALAAEQRKQGYRV 360
Cdd:PLN02530 379 GFGDAVIVELLKEKGLLPELPHQVDDVVFALDEDLqgaaaGVASRLREKGRSV 431
hisZ PRK12295
ATP phosphoribosyltransferase regulatory subunit; Provisional
70-326 1.44e-16

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183413 [Multi-domain]  Cd Length: 373  Bit Score: 80.36  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  70 DKEGHTLVLRPDVTTPFAR----VAASKllnnsPLRLAYEANVFRAQqreGGRPAEFEQIGVELIGDA-TMSSDAEVIAL 144
Cdd:PRK12295  54 DENGEELCLRPDFTIPVCRrhiaTAGGE-----PARYAYLGEVFRQR---RDRASEFLQAGIESFGRAdPAAADAEVLAL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 145 MIGALKRAGLKSFKVAIGHIG----FVNSLFL----------------------------EIVGNEERANVLRRFLYEKn 192
Cdd:PRK12295 126 ALEALAALGPGDLEVRLGDVGlfaaLVDALGLppgwkrrllrhfgrprsldallarlagpRVDPLDEHAGVLAALADEA- 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 193 yvGYRNHVKDLNLSS----------------IDKQRLLQLLNLRGDE--KKIE----------EAVELVEN---EAGKKA 241
Cdd:PRK12295 205 --AARALVEDLMSIAgispvggrspaeiarrLLEKAALAAAARLPAEalAVLErflaisgppdAALAALRAlaaDAGLDL 282
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 242 AGDLKKL---WNMLDAYGVtDEIKIDFNlVSH---MSYYTGILFEVFAENVGFH-IGNGGRYDQLLEKFASKT--PATGF 312
Cdd:PRK12295 283 DAALDRFearLAALAARGI-DLERLRFS-ASFgrpLDYYTGFVFEIRAAGNGDPpLAGGGRYDGLLTRLGAGEpiPAVGF 360
                        330
                 ....*....|....
gi 502824746 313 GIQLDRlIEALGEE 326
Cdd:PRK12295 361 SIWLDR-LAALGGA 373
hisZ PRK12293
ATP phosphoribosyltransferase regulatory subunit; Provisional
24-323 3.76e-06

ATP phosphoribosyltransferase regulatory subunit; Provisional


Pssm-ID: 183411  Cd Length: 281  Bit Score: 48.07  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  24 KKQVRNQLADEIGSWGYQYMATPTVEYYETVGSASAildQQLFKLLDKEGHTLVLRPDVTTPFARVAASKLL-NNSPLRL 102
Cdd:PRK12293  22 KREIENVASEILYENGFEEIVTPFFSYHQHQSIADE---KELIRFSDEKNHQISLRADSTLDVVRIVTKRLGrSTEHKKW 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 103 AYEANVFRAQQREggrpaeFEQIGVELIGDATMSsdaEVIALMIGALKRAGLKSFkVAIGHIGfVNSLFLEIVGNE---- 178
Cdd:PRK12293  99 FYIQPVFRYPSNE------IYQIGAELIGEEDLS---EILNIAAEIFEELELEPI-LQISNIK-IPKLVAEILGLDievf 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746 179 ERANVLRRFLYEKNYVGYRNHVKDLnlssidkqrllqllnlrgdeKKIEEAVELVENEAgkkaAGDLKKLWNmldaygVT 258
Cdd:PRK12293 168 KKGQIEKLLAQNVPWLNKLVRIKTL--------------------EDLDEVIELVPDEI----KEELEKLKE------LA 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502824746 259 DEIKIDfNLV------SHMSYYTGILFEVFAENvgFHIGNGGRYDqllekfASKTPATGFGIQLDRLIEAL 323
Cdd:PRK12293 218 ESIKYE-NLViaplyyAKMRYYDDLFFRFFDGN--STLASGGNYE------IDGISSSGFALYTDNLIEIL 279
class_II_aaRS-like_core cd00768
Class II tRNA amino-acyl synthetase-like catalytic core domain. Class II amino acyl-tRNA ...
24-151 7.51e-04

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: 40.56  E-value: 7.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502824746  24 KKQVRNQLAdeigSWGYQYMATPTVEYyETVGSASAILDQQLFKLLDKEGHTLVLRPdVTTPFARVAASKLLNNSPLRLA 103
Cdd:cd00768    6 EQKLRRFMA----ELGFQEVETPIVER-EPLLEKAGHEPKDLLPVGAENEEDLYLRP-TLEPGLVRLFVSHIRKLPLRLA 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 502824746 104 YEANVFRAQ--QREGGRPAEFEQIGVELIGDAtmSSDAEVIALMIGALKR 151
Cdd:cd00768   80 EIGPAFRNEggRRGLRRVREFTQLEGEVFGED--GEEASEFEELIELTEE 127
 
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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